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Papers In Press, published online ahead of print January 20, 2004
Biochemistry and Molecular Biology, University of New Hampshire, Durham, NH 03824
Corresponding Author: cldenis{at}cisunix.unh.edu
CCR4, a poly (A) deadenylase of the Exo III nuclease family, is a component of the multiprotein CCR4-NOT complex of Saccharomyces cerevisiae that is involved in mRNA degradation. CCR4, unlike all other Exo 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 (47/81) 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 a-helix/b-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 b-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 b-sheet surface of the LRR, including those which 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.
J. Biol. Chem, 10.1074/jbc.M313202200
Submitted on December 3, 2003
Revised on January 20, 2004
Accepted on January 19, 2004
Systematic mutagenesis of the leucine-rich repeat (LRR) domain of CCR4 reveals specific sites for binding to CAF1 and a separate critical role for the LRR in CCR4 deadenylase activity
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