Catalysis and substrate selection by histone/protein lysine acetyltransferases.
Catalysis and substrate selection by histone/protein lysine acetyltransferases.
复制标题
DOI:
10.1016/j.sbi.2008.11.004
复制
发表时间:
2008-12
影响因子:
6.8
通讯作者:
Denu, John M.
中科院分区:
文献类型:
--
作者:
Berndsen, Christopher E.;Denu, John M.
Reversible protein acetylation is controlled by the opposing actions of protein lysine acetyltransferases and deacetylations. Recent developments on the structure and biochemical mechanisms of histone acetyltransfers (HATs) have provided new insight into catalysis and substrate selection. Diverse families of HATs appear to perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex. In the case of newly discovered Rtt109 HAT, association with distinct histone chaperones directs substrate selection between N-terminal lysines (H3K9, H3K23) and those (H3K56) within the histone fold domain. Moreover, the ability of some HATs to utilize longer chain acyl-CoA (i.e. propionyl-CoA) as alternative substrates suggests a potential direct link between the metabolic state of the cell and transcriptional regulation.
登录
查看更多内容
DOI:
10.1126/science.1135862
发表时间:
2007-02-02
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
Driscoll R;Hudson A;Jackson SP
通讯作者:
Jackson SP
影响因子:
16
作者:
Clements, A;Poux, AN;Marmorstein, R
通讯作者:
Marmorstein, R
影响因子:
5.3
作者:
Asahara, H;Tartare-Deckert, S;Montminy, M
通讯作者:
Montminy, M
DOI:
10.1073/pnas.51.5.786
发表时间:
1964-01-01
影响因子:
11.1
作者:
ALLFREY, VG;FAULKNER, R;MIRSKY, AE
通讯作者:
MIRSKY, AE
影响因子:
56.9
作者:
Han, Junhong;Zhou, Hui;Zhang, Zhiguo
通讯作者:
Zhang, Zhiguo