Disrupt gene activity

Santisteban, M.S., Arents, G., Moudrianakis, E.N., and Smith, M.M. (1997) Histone octamer function in vivo mutations in the dimer-tetramer interfaces disrupt both gene activation and repression. EMBO J. 16, 2493-2506. 

Mandal, M., and Breaker, R. R. (2004). Adenine riboswitches and gene activation by disruption of a transcription terminator. Nat. Struct. Mol. Biol. 11, 29—35. 

Bodwell JE, Goose JA, Nomikos AP, Hamilton JW. Arsenic disruption of steroid receptor gene activation Complex dose-response effects are shared by several steroid receptors. Chem Res Toxicol 2006 19(12) 1619—29. 

The putative kinase domains are not highly conserved over evolution. The N-terminal kinase domain has weak similarity to a protein kinase family, whereas the C-terminal domains shows no similarity to any known kinase. Further characterization of the N-terminal kinase domain indicates that acidic residues in two small regions are important for the kinase activity (O Brien and Tjian, 1998). Combined mutation of both regions disrupts kinase activity, and the mutant has reduced ability to rescue the ts 13 cell line, a ts hamster cell line with a mutation in TAFl. This mutant shows a defect in transcription of approximately 6% in a genome-wide analysis (O Brien and Tjian, 2000), indicating that the kinase activity of the N-terminal domain may be required for expression of a subset of genes in vivo. 

Remodeling An ATP-dependent process of disrupting histone-DNA contacts in chromatin. Requires the action of dedicated macromolecular machines such as the SWI/SNF complex. An integral component of gene activation and repression. 

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