Research Project
Grant-in-Aid for Scientific Research (B)
In the eukaryotic nucleus, DNA exists as a nucleoprotein complex termed chromatin. The work is based on the hypothesis that chromatin dynamics and structure are an integral component of the analysis of DNA-dependent processes. Posttranslational histone modifications are important for the regulation of many biological phenomena. In this project, we clafified that a precise role for histone acetylation, namely to alter the structure of nucleosomes and facilitate the loss of H2A-H2B dimmers that have been previously remodeled by the action of ATP-dependent chromatin remodeling complexes. We also clarified that transcription from chromatin templates is ordered and sequential, with precise timing and roles for ATP-dependent chromatin remodeling, subsequent histone acetylation and alterations in nucleosome structure. In addition we found that histone H2A is phosphorylated by unique kinase. We found that NHK-1-catalyzed phosphorylation of a conserved serine/threonine residue in H2A is a new component of the histone code which might be related to cell cycle progression.
All 2004 2003 Other
All Journal Article Book Publications
Genes Dev 18
Pages : 877-888
J Biol Chem 279
Pages : 23661-23667
Biochem Biophys Res Commun 317
Pages : 259-264
Pages : 9698-9702
Cell 113
Pages : 905-917
Curr Top Microbiol Immunol 274
Pages : 1-22
実験医学 21
Pages : 1398-1401
Pages : 1402-1407
蛋白質核酸酵素 48
Pages : 2234-2240
Jikkenigaku 21
Tanpakushitu Kakusan Koso 48