Acetyl genes

Braunstein, M., Rose, A.B., Holmes, S.G., Allis, C.D. and Broach, J.R. (1993) Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes e[ Development, 7, 592-604. 

Weber WW. The Acetylator Gene and Drug Response. New York Oxford University Press, 1987. 

W.W. Weber, The Acetylator Genes and Drug Response, Oxford University Press, New York, 1987. 

Tan CH, Tay LK Tardive dyskinesia in elderly psychiatric patients in Singapore. Aust N Z J Psychiatry 25 119-122,1991 U.S. Bureau of the Census 1990 Summary Tape File 1C. Washington, DC, U.S. Bureau of the Census, 1990 Weber WW The Acetylator Genes and Drug Responses. New York, Oxford University Press, 1987... 

PABA, /7-aminobenzoic acid PAS, / -aminosalicylic acid PA, procainamide SMZ, sulphamethazine. Data from Weber (1987) The Acetylator Genes and Drug Response (New York Oxford University Press). 

Lee CH, Teng Q, Zhong RQ, Ye ZH. (2011). The four Arabidopsis reduced waU acetylation genes are expressed in secondary wall-containing cells and required for the acetylation of xylan. Plant Cell Physiol, 52(8), 1289-1301. 

The proportion of slow acetylators and the frequency of the slow acetylator gene has been determined in many different populations (see Table VIII). Frequencies of the slow acetylator phenotype range approximately from 5% in Canadian Eskimos (Armstrong and Peart, 1960) up to approximately 83% in Egyptians (Hashem et al., 1969). It can be seen from Table VIII that populations of Asiatic origin with few exceptions have low frequencies of the slow acetylator gene compared to populations of African and European origin and to Jewish populations which have been surveyed. 

Acylation of pyridazinethiones with acetyl chloride or benzoyl chloride gives the corresponding S-acylated products. 6-Mercaptopyridazine-3(2//)-thione gives either mono- or di-S-acylated products. A bispyridazinyl derivative is formed when phosgene or thiophos-gene is used as acylating agent. 

More subtle modes of action are also possible since the response to hormone receptor binding is complex and could be affected by chemical interference with receptor-related proteins, DNA methylation or histone acetylation. Dioxin (TCDD), for example, reduces the ability of the oestrogen-receptor complex to bind to the oestrogen response element of DNA, reducing gene transcription. ... 

JV-Acetyltransferases (NATs) catalyze the conjugation of an acetyl group from acetyl-CoA on to an amine, hydrazine or hydroxylamine moiety of an aromatic compound. NATs are involved in a variety of phase II-diug metabolizing processes. There are two isozymes NAT I and NAT II, which possess different substrate specificity profiles. The genes encoding NAT I and NAT II are both multi-allelic. Especially for NAT II, genetic polymoiphisms have been shown to result in different phenotypes (e.g., fast and slow acetylators). 

The major mechanism of resistance to chloramphenicol is mediated by the chloramphenicol acetyltransferases (CAT enzymes) which transfer one or two acetyl groups to one molecule of chloramphenicol. While the CAT enzymes share a common mechanism, different molecular classes can be discriminated. The corresponding genes are frequently located on integron-like structures and are widely distributed among Gramnegative and - positive bacteria. 

Clock gene and transcription factor with histone acetyl-transferase (HAT) activity that (in complex with BMAL1) constitutes a positive limb of molecular circadian oscillators. 

Histone acetylation is a reversible and covalent modification of histone proteins introduced at the e-amino groups of lysine residues. Histones and DNA form a complex - chromatin - which condenses DNA and controls gene activity. Current models interpret histone acetylation as a means to regulate chromatin activity. 

A model called histone code theory includes more aspects of chromatin regulation which have been identified. The histone code theory predicts that histone acetylation and other posttranslational histone modifications serve as binding sites for regulatory proteins which mediate processes like gene transcription upon recruitment (see Fig. 2b) [3]. In this context histone modifications can be understood as... 

Histone tails are the N-terminal regions of histones which reach outside the nucleosomes. They are not essential for the formation in of nucleosomes but are required for the formation of higher-order chromatin structures. The histone tails are also known to be heavily posttranslationally modified by acetylation, phosphorylation, methylation, etc. and are important for the regulation of gene activity. 

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