Title

Barrier-to-Autointegration Factor-Like (BAF-L) Interacts with Histones

Faculty Mentor(s)

Miriam Segura-Totten

Campus

Dahlonega

Subject Area

Biology

Location

Library Room 269:Open Classroom

Start Date

31-3-2014 12:00 PM

End Date

31-3-2014 1:30 PM

Description/Abstract

Barrier-to-Autointegration Factor (BAF) is a conserved DNA binding protein with cellular roles in nuclear assembly, regulation of chromatin structure, and gene expression. The regulation of chromatin structure by BAF is most likely mediated through its interactions with DNA and histones. BAF is regulated through phosphorylation, but there are other potential modifications of BAF that remain unknown. Barrier-to-Autointegration Factor-Like (BAF-L) is a protein that is 40% identical and 53% similar to BAF at the amino acid level. Recombinant BAF-L can form stable homodimers and can heterodimerize with BAF in vitro and in vivo. Although BAF-L does not significantly bind to DNA and other partners of BAF, it can interact with BAF in the presence of DNA. These distinct biochemical characteristics of BAF-L suggest that it might regulate BAF function through formation of BAF/BAF-L dimers. We hypothesize that binding of BAF-L may help regulate BAF interactions with histones and DNA. Preliminary data for our research group suggests that BAF-L can, like BAF, bind to histones H1 and H3. We will confirm this preliminary finding and extend it by testing BAF-L binding to histones through several protein-protein interaction assays.

Note to Conference Administrators

The University of North Georgia's Annual Research Conference is scheduled during the same time as another research conference many biology students attend, the Association of Southeastern Biologists (ASB) Research Conference. The presentations begin on April 3rd and April 4th for ASB. I am not sure how the presentations are scheduled as I have only presented in the poster session, but I would like to request that my presentation occur on either the 31st of March, or the 1st or 2nd of April if at all possible. Thank you for your time and consideration.

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Mar 31st, 12:00 PM Mar 31st, 1:30 PM

Barrier-to-Autointegration Factor-Like (BAF-L) Interacts with Histones

Library Room 269:Open Classroom

Barrier-to-Autointegration Factor (BAF) is a conserved DNA binding protein with cellular roles in nuclear assembly, regulation of chromatin structure, and gene expression. The regulation of chromatin structure by BAF is most likely mediated through its interactions with DNA and histones. BAF is regulated through phosphorylation, but there are other potential modifications of BAF that remain unknown. Barrier-to-Autointegration Factor-Like (BAF-L) is a protein that is 40% identical and 53% similar to BAF at the amino acid level. Recombinant BAF-L can form stable homodimers and can heterodimerize with BAF in vitro and in vivo. Although BAF-L does not significantly bind to DNA and other partners of BAF, it can interact with BAF in the presence of DNA. These distinct biochemical characteristics of BAF-L suggest that it might regulate BAF function through formation of BAF/BAF-L dimers. We hypothesize that binding of BAF-L may help regulate BAF interactions with histones and DNA. Preliminary data for our research group suggests that BAF-L can, like BAF, bind to histones H1 and H3. We will confirm this preliminary finding and extend it by testing BAF-L binding to histones through several protein-protein interaction assays.