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The Yeast Ccr4 Protein Is Neither Regulated by nor Associated with the Spt6 and Spt10 Proteins and Forms a Functionally Distinct Complex from That of the Snf/Swi Transcription Factors 总被引:2,自引:1,他引:1 下载免费PDF全文
C. L. Denis M. P. Draper H. Y. Liu T. Malvar R. C. Vallari W. J. Cook 《Genetics》1994,138(4):1005-1013
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Clark LB Viswanathan P Quigley G Chiang YC McMahon JS Yao G Chen J Nelsbach A Denis CL 《The Journal of biological chemistry》2004,279(14):13616-13623
CCR4, a poly(A) deadenylase of the exonuclease III family, is a component of the multiprotein CCR4-NOT complex of Saccharomyces cerevisiae that is involved in mRNA degradation. CCR4, unlike all other exonuclease III family members, contains a leucine-rich repeat (LRR) motif through which it makes contact to CAF1 and other factors. The LRR residues important in contacting CAF1 were identified by constructing 29 CCR4 mutations encompassing a majority (47 of 81) of residues interstitial to the conserved structural residues. Two-hybrid and immunoprecipitation data revealed that physical contact between CAF1 and the LRR is blocked by mutation of just two alpha-helix/beta-helix strand loop residues linking the first and second repeats. In contrast, CAF16, a potential ligand of CCR4, was abrogated in its binding to the LRR by mutations in the N terminus of the second beta-strand. The LRR domain was also found to contact the deadenylase domain of CCR4, and deletion of the LRR region completely inhibited CCR4 enzymatic activity. Mutations throughout the beta-sheet surface of the LRR, including those that did not specifically interfere with contacts to CAF1 or CAF16, significantly reduced CCR4 deadenylase activity. These results indicate that the CCR4-LRR, in addition to binding to CAF1, plays an essential role in the CCR4 deadenylation of mRNA. 相似文献
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Jan S. Fassler William Gray Jean Pyo Lee Guoying Yu Gregory Gingerich 《Molecular & general genetics : MGG》1991,230(1-2):310-320
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