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• W2017161857 abstract "The hamster histone H3.2 promoter contains a protein binding site (referred to as site X) required for G1/S transcriptional activation. We report here that nuclear extracts prepared from serum synchronized cells at various stages of the cell cycle show a blphasic increase In the H3.2 specific complex, H3abp, binding to site X. An Increase in binding activity occurs as cells first enter the cell cycle and later at the G1/S border. The H3.2 specific binding activity is enhanced by Mg 2+ and Ca 2+in vitro , but is inhibited by Zn 2+ . Site X resembles a Jun/AP-1 site, but previously it has been shown that the H3abp complex is immunologically distinct from the characterized AP-1 proteins. Here, we Identify the size of the hamster nuclear protein(s) that bind specifically to the H3abp site by ultra-violet crosslinking and renaturation of specific protein bands following gel electrophoresis. In addition, we purify H3abp by affinity chromatography and show that the purified H3abp has a different methylatlon Interference profile from AP-1. Our results indicate that a protein species around 68 kDa is the major DNA binding component of the H3abp complex and it binds specifically to the histone promoter site required for G1/S regulation." @default.
• W2017161857 created "2016-06-24" @default.
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• W2017161857 date "1995-01-01" @default.
• W2017161857 modified "2023-10-14" @default.
• W2017161857 title "Identification of a 68 kDa protein species as a specific DNA-binding component of the H3abp complex interacting with the histone H3.2 G1/S regulatory domain" @default.
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• W2017161857 doi "https://doi.org/10.1093/nar/23.3.475" @default.
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