Abstract
The interactions of nuclear lamins with the chromatin fiber play an important role in regulating nuclear architecture and chromatin function; however, the full spectrum of these interactions is not known. We report that the N-terminal domain of the nucleosome-binding protein HMGN5 interacts with the C-terminal domain of the lamin-binding protein LAP2α and that these proteins reciprocally alter their interaction with chromatin. Chromatin immunoprecipitation analysis of cells lacking either HMGN5 or LAP2α reveals that loss of either protein affects the genome-wide distribution of the remaining partner. Our study identifies a new functional link between chromatin-binding and lamin-binding proteins.
Highlights
HMGN5 is a nucleosome-binding protein that affects chromatin structure and function, and Lap2a is a lamin-binding protein that can bind to DNA
We report that the N-terminal domain of the nucleosome-binding protein HMGN5 interacts with the C-terminal domain of the lamin-binding protein LAP2␣ and that these proteins reciprocally alter their interaction with chromatin
Specific Interaction between HMGN5 and LAP2␣—To identify potential HMGN5 binding partners, we stably transfected HEK-293T cells with vectors expressing either HMGN5-Halo or unconjugated Halo tag and used HaloLink affinity chromatography of extracts from these cells to search for proteins that bound the HMGN5 protein
Summary
Background: HMGN5 is a nucleosome-binding protein that affects chromatin structure and function, and Lap2a is a lamin-binding protein that can bind to DNA. Results: HMGN5 and LAP2␣ interact and reciprocally affect each other’s genome-wide distribution. Chromatin immunoprecipitation analysis of cells lacking either HMGN5 or LAP2␣ reveals that loss of either protein affects the genome-wide distribution of the remaining partner.
Sign-in/Register to view highlights & summary 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.
