The Regulation of Gene Expression

Retinoic Acid Has a Role in the Regulation of Gene Expression Tissue Differentiation... 

Bogdan, C, 2001, Nitric oxide and the regulation of gene expression, Trends Cell Biol. 11 66-75. 

Shi Y, Lan L, Matson C, Mulhgan P, Whetstine JR, Cole PA, Casero RA, Shi Y (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSDl. Cell 119 941-953 Shilatifard A (2006) Chromatin Modifications by Methylation and Ubiquitination Implications in the Regulation of Gene Expression. Annu Rev Biochem 75 243-269 Sterner DE, Berger SL (2000) Acetylation of histones and transcription-related factors. Microbiol. Mol Biol Rev 64 435-459... 

Histone acetyltransferases (H ATs) catalyze the transfer of an acetyl moiety from acetyl-CoA to the E-amino group of certain lysine residues within core histone proteins. This transferase reaction produces acetylated histones and the deacetylated cofactor CoA-SH. As HATs are important enzymes in the regulation of gene expression, there are also a number of assays available to detect acetyltransferases activity. 

Histone methylation participates in the regulation of gene expression patterns. Unlike histone acetylation, histone methylation does not alter the charge of the amino acid and hence the histone tail. There are changes in the basicity and the hydrophobicity which are relatively small when viewed at the scale of the histone but still influence the affinity of the histone tails to certain proteins, for example transcription factors, which in turn result in certain signaling events. The histone methyltransferases are usually subdivided into three classes SET domain lysine methyltransfeases, nonSET domain lysine methyltransferases and arginine methyltransferases (PRMTs). All of them utilize S-adenosylmethionine (SAM) as cosubstrate for the methylation reaction... 

The requirement for zinc in the regulation of gene expression is exemplified by transcription factor IIIA, which has been shown to contain from two (Hanas et al., 1983) to seven to eleven (Miller et al., 1985) zinc ions bound to a 40K protein molecule. Transcription factor IIIA is obtained from immature Xenopus oocytes in a complex with 5 S RNA, and the protein is required for transcription initiation the apoprotein does not bind to the 5 S RNA gene (Hanas et al, 1983). Uncertainties regarding the stoichiometric requirement for zinc persist, given the report by Shang et al. (1989) that transcription factor IIIA, as either the isolated protein or the 5 S RNA complex, contains two firmly bound zinc ions which are required for transcription activation. 

Bogdan C (2001) Nitric oxide and the regulation of gene expression. Trends Cell Biol 11 66-75 Bourtchuladze R, Frenguelli B, Blendy J, Cioffi D, Schutz G, SUva AJ (1994) Deficient longterm memory in mice with a targeted mutation of the cAMP-responsive element-binding protein. Cell 79 59-68... 

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