Abstract
Post-translational modifications of histones are known to be an important mechanism for the precise regulation of chromatin structure. These modifications influence the ability of chromatin to function as a template for cellular processes. Recently, histone biotinylation has been added to the other known modifications, and shown to be of cellular significance. There is accumulating evidence that histone biotinylation is catalyzed by the enzyme holocarboxylase synthetase (HCS). HCS protein lacks well-characterized nuclear localization signal and DNA-binding domains, suggesting that it could require other cellular factors for its putative translocation to the nucleus and its targeting to specific regions of chromatin. Here we used yeast two hybrid screening to identify proteins that interact with HCS to discover ones that could have possible roles in directing HCS from cytoplasm to cell nucleus and/or recruiting HCS to certain regions of chromatin. Initial screening revealed 22 different proteins that potentially interacted with HCS. Among these were two zinc finger proteins. This work will report on the further characterization of these interactions. This work was supported by NIH grants DK 063945 and ES 015206-01, USDA grant 2006-35200-01540, and by NSF EPSCoR grant EPS-0346476.
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