The hydrophobic patch of ubiquitin is required to protect transactivator-promoter complexes from destabilization by the proteasomal ATPases.
The hydrophobic patch of ubiquitin is required to protect transactivator-promoter complexes from destabilization by the proteasomal ATPases.
复制标题
需要泛素的疏水性片段来保护反式激活子-启动子复合物免受蛋白酶体 ATP 酶的破坏。
DOI：
10.1093/nar/gkp1066
复制
发表时间：
2010
影响因子：
14.9
通讯作者：
Kodadek,Thomas
中科院分区：
文献类型：
--
作者：
Archer,ChaseT;Kodadek,Thomas
Mono-ubiquitylation of a transactivator is known to promote transcriptional activation of certain transactivator proteins. For theSacchromyces cerevisiaetransactivator,GAL4, attachment of mono-ubiquitin prevents destabilization of the DNA–transactivator complex by the ATPases of the 26S proteasome. This inhibition of destabilization depends on the arrangement of ubiquitin; a chain of ubiquitin tetramers linked through lysine 48 did not display the same protective effect as mono-ubiquitin. This led to an investigation into the properties of ubiquitin that may be responsible for this difference in activity between the different forms. We demonstrate the ubiquitin tetramers linked through lysine 63 do protect from proteasomal-mediated destabilization. In addition, we show that the mutating the isoleucine residue at position 44 interferes with proteasomal interactionin vitroand will abolish the protective activityin vivo. Together, these data implicate the hydrophobic patch of ubiquitin as required to protect transactivators from destabilization by the proteasomal ATPases.
