Abstract
The Hat1 chromatin assembly complex contains the Hat1 histone acetyltransferase and two Hat1‐interacting factors: Hat2 and Hif1. The Hat1 complex specifically acetylates histone H4 and is part of a pathway that deposits newly synthesized histone H3 and histone H4 onto DNA during chromatin assembly. In yeast, Hat1 complexes contribute to gene regulation and DNA repair. Hat1, Hat2 and Hif1 are each highly conserved and form similar complexes in organisms ranging from yeast to humans. We are using biochemical and biophysical methods to study the structure and function of the Hif1 protein from yeast with the goal of understanding how it contributes to the activity of the Hat1 chromatin assembly complex. Hif1 contains four tetratricopeptide (TPR) sequence motifs, binds histones and has histone chaperone activity. Bacterially expressed yeast Hif1 is an oligomer, forming dimers and possibly tetrameric assemblies, and interacts with histones. A truncation mutant consisting of only the TPR sequence motifs of Hif1 is also an oligomer and retains histone binding activity. We are currently testing further truncation mutants to delineate the Hif1 region(s) responsible for oligomer formation and histone binding.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
