Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 73, Issue 2, Pages 378-384Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.80621
Keywords
Saccharomyces cerevisiae; histone deacetylase; HDAC; Rpd3L; RPD3
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [19580107, 19780076]
- Grants-in-Aid for Scientific Research [19580107, 19780076] Funding Source: KAKEN
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In eukaryotes, the hypoacetylated state of histone N-terminal lysines at many gene-promoters, which is created by histone deacetylases (HDACs), is changed to the hyperacetylated state by the function of histone acetyltransferases (HATs) upon transcription activation. Although much insight has been obtained to date as to how modification of the histone tail regulates gene expression, little is known about how the transition between the unmodified and modified states takes place. In Saccharomyces cerevisiae, the HDAC complex containing Rpd3 (Rpd3L) represses the transcription of several sets of genes through the URSI cis-element. We found that the histone H3 acetylation level at the URSI of seven genes (INO1, CAT2, ACS1, YAT1, RIM4, CRC1, and SIP4) was elevated in the presence of Rpd3/HDAC in growth in acetate-containing medium (YPA), suggesting that a mechanism that regulates HDAC activity is present in this organism. The biological significance of this phenomenon is discussed below.
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