Medical Research Council Laboratory Research Articles

Milstein and Kohler: Monoclonal Antibodies.

César Milstein (1927-2002) was born in Bahía Blanca, Argentina. He was a chemistry student educated at the University of Buenos Aires, obtaining his degree in biochemistry in 1952. He completed his PhD in 1957 at the same University and also received the British Council research scholarship to the biochemistry department at the University of Cambridge. Under the direction of the distinguished biochemist Frederick Sanger, Milstein completed a second dissertation, a study of the enzyme, earning his PhD in 1960 and joining the scientific staff of the Medical Research Council (MRC). He then worked at the National Institute of Microbiology in Buenos Aires from 1961 to 1963 until political turmoil led him to resign and return to Cambridge to work with Sanger at the newly formed MRC Laboratory of Molecular Biology. Now, he shifted his focus from enzymes to antibodies. By the early 1970s, he was an internationally recognized leader in the field and was able to attract talented, young researchers, including Georges Köhler, to the MRC. In 1983, Milstein was named head of the Protein and Nucleic Acid Chemistry Division of the MRC, a position he held until his retirement in 1995. He died in Cambridge, England, in 2002 at the age of 74.

Andrew David McLachlan. 25 January 1935—8 July 2022

Andrew McLachlan enjoyed a wide-ranging career, starting as a theoretical chemist and ending as a molecular biologist. After reading physics as an undergraduate at Trinity College, Cambridge, he joined the Theoretical Chemistry Section of the Chemistry Department to study for a PhD. His work on electron spin resonance then led to his election as a research fellow at Trinity. Following postdoctoral work in the United States, he returned to Cambridge as a college lecturer in physics at Trinity and was eventually appointed a university lecturer in chemistry. Despite a productive research programme in various aspects of theoretical chemistry, he decided that a move into the newly developing subject of molecular biology would provide an exciting opportunity. Accordingly, in 1967 he accepted an offer to join the Medical Research Council Laboratory of Molecular Biology. The initial plan was to work on the mechanism of oxygen uptake by haemoglobin, but he quickly became interested in wider problems of protein structure. In particular, he developed methods for aligning the sequences of different proteins and for detecting repeated sequences and motifs, leading to an interest in the evolution of protein sequences. In collaboration with others, he applied his methods to a wide range of proteins, providing important understanding of their structures and relationships.

First person – Sherman Foo

ABSTRACT First Person is a series of interviews with the first authors of a selection of papers published in Journal of Cell Science, helping researchers promote themselves alongside their papers. Sherman Foo is first author on ‘ Diacylglycerol at the inner nuclear membrane fuels nuclear envelope expansion in closed mitosis’, published in JCS. Sherman conducted the research described in this article while a PhD student in the labs of Snezhana Oliferenko (The Francis Crick Institute, London, UK, and Randall Centre for Cell and Molecular Biophysics, King's College London, UK) and Markus R. Wenk (Singapore Lipidomics Incubator, National University of Singapore). He is now a postdoc in the lab of Buzz Baum at Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, UK, where he is currently studying cellular organization of hyperthermophilic archaea, with a particular focus on the surface layer and cell cycle of Sulfolobus acidocaldarius.

Using T4 genetics and Laemmli’s development of high-resolution SDS gel electrophoresis to reveal structural protein interactions controlling protein folding and phage self-assembly

One of the most transformative experimental techniques in the rise of modern molecular biology and biochemistry was the development of high-resolution sodium dodecyl sulfate polyacrylamide gel electrophoresis, which allowed separation of proteins—including structural proteins—in complex mixtures according to their molecular weights. Its development was intimately tied to investigations of the control of virus assembly within phage-infected cells. The method was developed by Ulrich K. Laemmli working in the virus structural group led by Aaron Klug at the famed Medical Research Council Laboratory for Molecular Biology at Cambridge, UK. While Laemmli was tackling T4 head assembly, I sat at the next bench working on T4 tail assembly. To date, Laemmli’s original paper has been cited almost 300,000 times. His gel procedure and our cooperation allowed us to sort out the sequential protein–protein interactions controlling the viral self-assembly pathways. It is still not fully appreciated that this control involved protein conformational change induced by interaction with an edge of the growing structure. Subsequent efforts of my students and I to understand how temperature-sensitive mutations interfered with assembly were important in revealing the intracellular off-pathway aggregation processes competing with productive protein folding. These misfolding processes slowed the initial productivity of the biotechnology industry. The article below describes the scientific origin, context, and sociology that supported these advances in protein biochemistry, protein expression, and virus assembly. The cooperation and collaboration that was integral to both the Laboratory for Molecular Biology culture and phage genetics fields were key to these endeavors.

Walter Bruno Gratzer (1932–2021): In his own words, as far as possible

Miranda Robertson commemorates the life, remarkable times and witty and erudite writing of protein chemist and biophysicist Walter Gratzer.

Sir Dai Rees (28 April 1936 to 10 June 2021)

Sir Dai Rees (28 April 1936 to 10 June 2021)

The 2021 FASEB Virtual Science Research Conference on Protein Aggregation: Function, Dysfunction, and Disease, June 23-25, 2021.

The 2021 FASEB Virtual Science Research Conference on Protein Aggregation: Function, Dysfunction, and Disease, June 23-25, 2021.

Cell scientist to watch – Hayley Sharpe

ABSTRACT Hayley Sharpe graduated from the University of Bath, UK, with a degree in biochemistry. She then joined the laboratory of Sean Munro for her PhD in cell and molecular biology at the Medical Research Council Laboratory of Molecular Biology (MRC-LMB) in Cambridge, UK. There, she investigated the properties of protein transmembrane domains embedded within the organelle membranes of the secretory pathway. She next moved to San Francisco, USA, for postdoctoral work at Genentech, where she studied clinical resistance mechanisms to a Hedgehog pathway inhibitor in skin cancer. In 2016, Hayley returned to the UK to establish her own research group at the Cambridge Institute for Medical Research, and in 2019, she moved to the Babraham Institute, also in Cambridge. Her laboratory works on understanding how protein tyrosine phosphatases function in signalling and cell–cell communication, with a particular focus on a family of cell surface receptors. Hayley became part of the EMBO Young Investigator Programme in 2019 and was awarded the Lister Institute Research Prize in 2020.

Industrial cryo-EM facility setup and management.

Cryo-electron microscopy (cryo-EM) has rapidly expanded with the introduction of direct electron detectors, improved image-processing software and automated image acquisition. Its recent adoption by industry, particularly in structure-based drug design, creates new requirements in terms of reliability, reproducibility and throughput. In 2016, Thermo Fisher Scientific (then FEI) partnered with the Medical Research Council Laboratory of Molecular Biology, the University of Cambridge Nanoscience Centre and five pharmaceutical companies [Astex Pharmaceuticals, AstraZeneca, GSK, Sosei Heptares and Union Chimique Belge (UCB)] to form the Cambridge Pharmaceutical Cryo-EM Consortium to share the risks of exploring cryo-EM for early-stage drug discovery. The Consortium expanded with a second Themo Scientific Krios Cryo-EM at the University of Cambridge Department of Materials Science and Metallurgy. Several Consortium members have set up in-house facilities, and a full service cryo-EM facility with Krios and Glacios has been created with the Electron Bio-Imaging Centre for Industry (eBIC for Industry) at Diamond Light Source (DLS), UK. This paper will cover the lessons learned during the setting up of these facilities, including two Consortium Krios microscopes and preparation laboratories, several Glacios microscopes at Consortium member sites, and a Krios and Glacios at eBIC for Industry, regarding site evaluation and selection for high-resolution cryo-EM microscopes, the installation process, scheduling, the operation and maintenance of the microscopes and preparation laboratories, and image processing.

Taking a confident leap into uncertainty.

Melina Schuh did her PhD at the European Molecular Biology Laboratory with Jan Ellenberg. She became group leader at the Medical Research Council Laboratory of Molecular Biology in Cambridge, UK, in 2009, and was appointed Director at the Max Planck Institute for Biophysical Chemistry in Gottingen, Germany, in 2016.

A different perspective on the brain

Five contemporary artists, who collaborated with scientists to explore current biological research, showcased their works as part of the Brilliant Brains exhibition at the Cambridge Science Festival (Cambridge, UK), whose theme was “making sense of the brain”. Intended originally for a neutral gallery environment, the selection and display were rethought for an alternative space—where bookshelves and furniture evoked an old-fashioned library—late in the curatorial process. This was an appropriate setting for the ingenious thought-provoking works resulting from the five artist–scientist pairings, three of which engaged directly with human consciousness and are reviewed here. “I started to see the brain as a representation of an inner space; vastly complex and uncharted as a field of exploration”, says artist Sarah Harley. Her exhibited works result from collaboration with Srivas Chennu (University of Cambridge, UK), whose research into alterations in brain activity in minimally conscious states has shown how EEG can be used to characterise brain networks, measure cognition, and detect awareness in patients in vegetative states. Harley's use of textiles in conjunction with printmaking adds a domestic familiarity and intimacy to her cloud-shaped etchings and monoprints of brains. Various 3D mixed-media works are displayed on crocheted doilies, whose scalloped forms and intricately linked threads evoke the brain's gross anatomy and its myriad interconnected neurons. The search for your spark, a lidded glass jar filled with water, represents the sense of separation and unreachability of patients in vegetative states. White threads, some tipped with gold leaf, float above a white porcelain head submerged at the bottom of the jar. The entangled threads and their gold tips refer respectively to cerebral neurons and neural transmission. “Floating flecks of gold leaf refer to the urge to shake a person to wake them or bring them into a conscious state”, Harley explains. “I am particularly interested in the complex dynamics between body and mind, perception, and knowledge”, says artist Charlotte Morrison. Her exhibited works were inspired by her collaboration with Madeline Lancaster (Medical Research Council Laboratory of Molecular Biology, Cambridge, UK), who grows in vitro 3D tissues called cerebral organoids (so-called mini-brains). Generated from human pluripotent stem cells, they are used in studying the stages of human brain development microscopically. Morrison's artwork Making Brains shadows Lancaster's methodology in two stages. First, she creates 3D disks by building up layers of glue and ink on Perspex. Then, using a rectangular light-impermeable template with four circular openings, she positions her “glue brains” on sheets of light-sensitive paper. By exposing the Perspex disks to light, she captures their inner structures as cyanotype prints. Works created by Sally Stenton in collaboration with neuroscientist Marty Fiati (Anglia Ruskin University, Cambridge, UK) connect both with our perception of places and of the movement between them. The Forensic Corridor, displayed horizontally across three shelves of adjacent bookcases, presents her “walk from art to science and back again”. Strapping a smartphone to her belt, she recorded a video of her return journey between the Cambridge School of Art and the Faculty of Science and Technology building at Anglia Ruskin University. Using two facing projectors, flickering footage of her outbound walk was projected from left to right on the left-hand shelf, and her return footage was projected from right to left on the right-hand one. The intermediary shelf was filled with an eclectic selection of appropriately titled books, chosen by the artist and the scientist, including The Mind at Night, Fleeting Memories, Neurophysiology of Vision, and Memory, Aging and The Brain. Art theory titles were also borrowed from the Ruskin Gallery. Displayed in this library setting, the artist's walk suggests that the “two cultures” of art and science famously described by C P Snow are easily bridged, at least in this university town. Trying to read your thoughts, Harley's tiny handmade book provides the final word in this intriguing exhibition. It was made by stitching blank white embossed pages between endpapers and covers, printed with etched fragments of grey doilies, and embroidering “your beautiful brain”' in red thread on its front cover. When fanned open, the contours embossed onto its pages evoke convoluted folds in sections of cerebral cortex, while their blank whiteness hints at what is still unknown about the brain and its function. It's a mute but eloquent comment on the adjacent bookshelves, crammed with research findings and scholarly conjecture on human consciousness, mind, and matter. Brilliant Brains: seeing science through art CB2 Restaurant Café, Cambridge, UK, March 12–18, 2018, during the Cambridge Science Festival Brilliant Brains: seeing science through art CB2 Restaurant Café, Cambridge, UK, March 12–18, 2018, during the Cambridge Science Festival

Profile of Joachim Frank, Richard Henderson, and Jacques Dubochet, 2017 Nobel Laureates in Chemistry

In 2017, the Nobel Prize in Chemistry was awarded to three key pioneers in the birth and development of cryoelectron microscopy (cryo-EM): Jacques Dubochet, Joachim Frank, and Richard Henderson. As a starting graduate student in England, moving from physics to biology and the study of macromolecular structure, I had the fortune of attending one of the early conferences in the, at the time, embryonic field of cryo-EM. It was 1990, and Jacques Dubochet (Fig. 1), whom I met at the conference, and coworkers (1) had provided the scientific community a few years before with a simple, highly practical way to “vitrify” solutions of biological samples that they used, for example, to visualize intact viral particles (2). Dubochet’s charming recounting of the early days in his own words can be found in a recent perspective (3). By then, there was already access to commercially available cryoholders to use standard transmission electron microscopes for the study of frozen-hydrated samples. Thus, major practical bottlenecks had already been overcome, but the cryo-EM community could still be counted on one’s fingers. That year of 1990 saw the publication of the long-time-coming atomic model of bacteriorhodopsin using electron crystallography (not quite vitrified, discussed below) by Henderson et al. (4) (Fig. 2). This publication was the needed demonstration that electrons could provide this kind of detailed structural description of radiation-sensitive biological samples. That paper became a true inspiration for me and for a whole generation of cryo-EM practitioners. Fig. 1. Jacques Dubochet. Image courtesy of Felix Imhof (photographer), © Universite de Lausanne (UNIL). Fig. 2. Richard Henderson. Image courtesy of Medical Research Council (MRC) Laboratory of Molecular Biology. While there was a very long history of the electron microscope’s use to visualize both cellular ultrastructure and molecular architecture, few were aware, at the time, of the capabilities of the technique to … [↵][1]1Email: enogales{at}lbl.gov. [1]: #xref-corresp-1-1

Janitorial system in red blood cells discovered

Red blood cells are a stripped-down version of most other cells: The oxygen-carrying workhorses are packed with hemoglobin and little else. As immature red blood cells called reticulocytes transform into dedicated oxygen carriers, they trash their nucleus, organelles, and most proteins. Two groups of scientists are now reporting that this massive and selective clearance event occurs thanks to a protein degradation pathway involving an enzyme called UBE2O. A team led by Daniel Finley and Mark D. Fleming at Harvard Medical School report that in the last stages of red blood cell differentiation, UBE2O remodels the proteome inside reticulocytes by tagging the small protein ubiquitin onto protein “trash” to signal for its breakdown, leaving the cell with approximately 98% α- and β-globin, the subunits that join to form hemoglobin (Science 2017, DOI: 10.1126/science.aan0218). Meanwhile, Ramanujan S. Hegde and his team at the Medical Research Council Laboratory of Molecular Biology in Cambridge,

Biology, wet and dry

Sarah Teichmann's work on how cells regulate gene expression and build protein complexes recently won her a European Molecular Biology Organization Gold Medal. At 40, Teichmann holds a joint appointment with the European Bioinformatics Institute and the Wellcome Trust Sanger Institute in Hinxton, U.K. She leads a systems biology group of 17 researchers that uses both computational methods and lab experimentation. Science Careers asked Teichmann how she combines the two approaches. This interview has been edited for clarity and brevity. Q: What came first, informatics or biology? A: Biology, but informatics has always been at the heart of my research. I felt inspired by computational biology when, as an undergraduate, I read a 1992 commentary by Cyrus Chothia where he made a simple calculation of the likely number of protein families. I felt excited about discovering general principles in biology and became convinced that computational biology would provide the necessary tools. By the time I started looking for a Ph.D. in the mid-1990s, data sets had become large enough to gain a global view of the protein structure universe and of protein and gene sequences. So I went to work with Chothia at the Medical Research Council Laboratory of Molecular Biology in Cambridge, exploring protein families and the domain organization of proteins in the first completely sequenced genomes. ![Figure][1] ILLUSTRATION: ROBERT NEUBECKER > “What unifies both wet and dry work is the conceptual part of the science.” Q: Was computational biology a risky career choice? A: Yes. But I never looked back, even though at one point I came to feel that computational biology and bioinformatics were viewed as eccentric and unorthodox. My Ph.D. mentor exuded such unwavering optimism and confidence, however, that it made his lab a great place to work. Altogether, during my Ph.D., I published 10 papers. Q: What are the pros and cons of combining computational and experimental approaches? A: The beauty of a “wet-dry” group is that you have the ability to interpret your own experimental data computationally and to test computational predictions experimentally. The challenge, however, is maintaining the right balance and harnessing the potential of both sides of the group. Q: How did you learn these two approaches? A: During my first degree in the natural sciences at the University of Cambridge, I took math, physics, chemistry, and biology at a high level. I built on this through short courses and learning by doing. Today, I'd recommend more structured courses in algorithms and programming. Q: How do you feel about experimental work? A: I discovered early on that my fine motor skills are not up to some of the very tricky handling needed to be a top experimentalist in molecular biology. I have huge respect and gratitude for people who generate data through wet-lab experiments. What unifies both wet and dry work is the conceptual part of the science, which has to be logical and original, and both require exceptional dedication. Q: Is there anything you wish you had done differently? A: I made career choices mostly based on the package and colleagues I would have. In retrospect, it is also important to consider questions such as whether the scientific strategy and values of an institute are aligned with your own. I've also learned to shed my introverted nature and appreciate how important it is to talk to people often and openly. Q: Has it been hard to maintain a good work-life balance? A: Yes. I have two young daughters, and I believe that our society is a long way from empowering both men and women to balance their professional and family lives. There should be financial and cultural support for both men and women to work shorter hours for several months after the birth of an infant. Ultimately, fair and equal treatment would decrease unconscious bias in all of us. [1]: pending:yes

ISMB/ECCB Rebooted: 2015 Brings Major Update to the Meeting Program

The 23rd Annual International Conference on Intelligent Systems for Molecular Biology and the 14th European Conference on Computational Biology (ISMB/ECCB 2015) is shaping up to be a phenomenal meeting, with world-renowned keynote speakers and changes in the meeting format that aim to make it a more streamlined and user-friendly conference. The joint ISMB/ECCB conference is held biennially and is the flagship meeting of the International Society for Computational Biology (ISCB). The meeting will take place at the Convention Center Dublin, Ireland, from July 10–14, 2015, and will bring together scientists from across the globe working in a broad range of computational biology—related disciplines, including genomics, structural biology, proteomics, data mining, machine learning, and systems biology. Online registration is open until June 26: https://www.iscb.org/ismbeccb2015-registration. In the past, presentations at the meeting have been organized according to tracks, namely, the Proceedings, Highlights, and Late Breaking Research tracks. In 2015, all oral presentations will be presented in broad thematic areas. As in the past, submissions accepted into the highly selective Proceedings track will be published in a special ISMB/ECCB Proceedings issue of Bioinformatics. Conference co-chairs Alex Bateman, Janet Kelso, and Des Higgins and the conference committee undertook the reorganization effort and came up with five thematic areas: Genes, Proteins, Systems, Disease, and Data. Batemen said, “The idea of themes is an obvious way to organize the talks. But, selecting a small number of themes that represented all computational biology was challenging. Of course, many talks will potentially fit across several themes. Time will tell whether these need any tweaking for future meetings.” Kelso believes the new organization will benefit attendees and said, “We hope that organizing the meeting more thematically will mean that attendees have an easier time identifying sessions that are relevant and interesting to them.” As in the past, the keynote speaker lineup features world-class scientists. The speakers include Amos Bairoch of the Swiss Institute of Bioinformatics (ISCB Fellows Keynote), Cyrus Chothia of the Medical Research Council (MRC) Laboratory of Molecular Biology (Senior Scientist Award winner), Eileen Furlong of the European Molecular Biology Laboratory, Curtis Huttenhower of the Harvard T. H. Chan School of Public Health (Overton Prize winner), 2013 Nobel Laureate Michael Levitt of Stanford University, and Kenneth Wolfe of University College Dublin. The main conference program takes place from Sunday, July 12, through Tuesday, July 14. In the tradition of previous ISMB/ECCB meetings, special interest group and satellite meetings will occur prior to the conference on Thursday, July 10, and Friday, July 11. This year, the tutorials and workshops that usually precede the main meeting are being replaced by applied knowledge exchange sessions (AKES). The AKES are scheduled for Saturday, July 11, and are designed to provide interactive educational and knowledge exchange opportunities for attendees. AKES will also provide a chance for junior principle investigators to meet and exchange career advice. Six AKES have been scheduled: AKES 01: Applied Knowledge Building Networks for Translation: How to Use DREAM Challenges and the Synapse Platform as a Research Strategy AKES 02: Cytoscape 3 App Development: Variations on a Theme—“Hello World” AKES 03: Bioinformatics Software Testing and Quality Assurance AKES 04: Using Biological Cyberinfrastructure to Scale Science and People—Applications in Data Storage, HPC (High-Performance Computing), Cloud Analysis, and Bioinformatics Training AKES 05: Open-Access, Cloud-Based, Individual-Level Clinical Trials Data—Sharing, Dissemination and Analyses AKES 06: Junior Principal Investigator ISMB/ECCB 2015 will also include special sessions, poster presentations in the exhibit hall, the Student Council Symposium, and social activities. This year’s meeting promises to be an eagerly anticipated reboot of ISMB/ECCB, with great science and collaboration at its core.

Message from the ISCB: 2015 ISCB Accomplishment by a Senior Scientist Award: Cyrus Chothia.

The International Society for Computational Biology (ISCB; http://www.iscb.org) honors a senior scientist annually for his or her outstanding achievements with the ISCB Accomplishment by a Senior Scientist Award. This award recognizes a leader in the field of computational biology for his or her significant contributions to the community through research, service and education. Cyrus Chothia, an emeritus scientist at the Medical Research Council Laboratory of Molecular Biology and emeritus fellow of Wolfson College at Cambridge University, England, is the 2015 ISCB Accomplishment by a Senior Scientist Award winner.Chothia was selected by the Awards Committee, which is chaired by Dr Bonnie Berger of the Massachusetts Institute of Technology. He will receive his award and deliver a keynote presentation at 2015 Intelligent Systems for Molecular Biology/European Conference on Computational Biology in Dublin, Ireland, in July 2015. dkovats@iscb.org.

Cellular Incorporation of Unnatural Amino Acids and Bioorthogonal Labeling of Proteins

ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTCellular Incorporation of Unnatural Amino Acids and Bioorthogonal Labeling of ProteinsKathrin Lang* and Jason W. Chin*View Author Information Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom*E-mail: [email protected]*E-mail: [email protected]Cite this: Chem. Rev. 2014, 114, 9, 4764–4806Publication Date (Web):March 21, 2014Publication History Received4 July 2013Published online21 March 2014Published inissue 14 May 2014https://doi.org/10.1021/cr400355wCopyright © 2014 American Chemical SocietyRIGHTS & PERMISSIONSArticle Views31250Altmetric-Citations738LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit Read OnlinePDF (17 MB) Get e-AlertsSUBJECTS:Azides,Fluorescence,Labeling,Monomers,Peptides and proteins Get e-Alerts

Histone H3 Lysine 14 (H3K14) Acetylation Facilitates DNA Repair in a Positioned Nucleosome by Stabilizing the Binding of the Chromatin Remodeler RSC (Remodels Structure of Chromatin)

Histone H3 acetylation is induced by UV damage in yeast and may play an important role in regulating the repair of UV photolesions in nucleosome-loaded genomic loci. However, it remains elusive how H3 acetylation facilitates repair. We generated a strongly positioned nucleosome containing homogeneously acetylated H3 at Lys-14 (H3K14ac) and investigated possible mechanisms by which H3K14 acetylation modulates repair. We show that H3K14ac does not alter nucleosome unfolding dynamics or enhance the repair of UV-induced cyclobutane pyrimidine dimers by UV photolyase. Importantly, however, nucleosomes with H3K14ac have a higher affinity for purified chromatin remodeling complex RSC (Remodels the Structure of Chromatin) and show greater cyclobutane pyrimidine dimer repair compared with unacetylated nucleosomes. Our study indicates that, by anchoring RSC, H3K14 acetylation plays an important role in the unfolding of strongly positioned nucleosomes during repair of UV damage.

A tribute to Michael S. Neuberger

A tribute to Michael S. Neuberger

Colin Russell Austin 1914–2004

Colin Russell Austin, English by birth, initially graduated in Veterinary Science from the University of Sydney in 1936. The Second World War limited his career options, but he was fortunate to be employed by the CSIR Division of Animal Health in Sydney. In 1954 he was invited to join the staff of the Medical Research Council's laboratory in Mill Hill, London to study fertilization and early embryonic development in rats and rabbits. As a result, in 1962 he was asked to teach Fertilization and Gamete Physiology at the Marine Biological Laboratory, Woods Hole, Massachusetts, and subsequently became Professor of Embryology in the Medical School at Tulane University, New Orleans. This alerted the University of Cambridge to his potential and they created a special Charles Darwin Chair for him in 1967. This enabled him to support the work of his young student Robert Edwards on human in vitro fertilization and embryonic development that culminated in the award of the Nobel Prize to Edwards and Patrick Steptoe in 2010. Austin also devoted a great deal of his time to editing the 13-volume Cambridge University Press series of textbooks, Reproduction in Mammals, completing the series from his retirement home in Buderim, Queensland in 1986.