The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex.
作者： Olesya Panasenko , Emilie Landrieux , Marc Feuermann , Andrija Finka , Nicole Paquet
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摘要: In this work, we determine that the Saccharomyces cerevisiae Ccr4-Not complex controls ubiquitination of conserved ribosome-associated heterodimeric EGD (enhancer Gal4p DNA binding) complex, which consists Egd1p and Egd2p subunits in yeast is named NAC (nascent polypeptide-associated complex) mammals. We show are ubiquitinated proteins, whose status regulated during cell growth. has a UBA domain not essential for interaction with but required stability Egd1p. Ubiquitination requires Not4p. also Not4p, an intact Not4p RING finger domain, all other tested. absence mislocalizes to punctuate structures. Finally, can be vitro by Ubc4p, one E2 enzymes interact. Taken together our results reveal manner, they new role ubiquitination.
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