Nucleic Acids Research Advance Access originally published online on January 30, 2007
Nucleic Acids Research 2007 35(4):1108-1118; doi:10.1093/nar/gkl1160
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Nucleic Acids Research, 2007, Vol. 35, No. 4 1108-1118
© 2007 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Functional overlap between conserved and diverged KH domains in Saccharomyces cerevisiae SCP160
1Graduate Program in Genetics and Molecular Biology, Emory University 2Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322 and 3Department of Human Genetics, Emory University School of Medicine, Atlanta, GA 30322, USA
*To whom correspondence should be addressed. Tel: +1 404 727 3924; Fax: 404 727 3949; Email: jfridov{at}emory.edu
Received September 13, 2006. Revised December 20, 2006. Accepted December 20, 2006.
The K homology (KH) domain is a remarkably versatile and highly conserved RNA-binding motif. Classical KH domains include a characteristic pattern of hydrophobic residues, a Gly-X-X-Gly (GXXG) segment, and a variable loop. KH domains typically occur in clusters, with some retaining their GXXG sequence (conserved), while others do not (diverged). As a first step towards addressing whether GXXG is essential for KH-domain function, we explored the roles of conserved and diverged KH domains in Scp160p, a multiple-KH-domain-containing protein in Saccharomyces cerevisiae. We specifically wanted to know (1) whether diverged KH domains were essential for Scp160p function, and (2) whether diverged KH domains could functionally replace conserved KH domains. To address these questions, we deleted and/or interchanged conserved and diverged KH domains of Scp160p and expressed the mutated alleles in yeast. Our results demonstrated that the answer to each question was yes. Both conserved and diverged KH domains are essential for Scp160p function, and diverged KH domains can function in place of conserved KH domains. These findings challenge the prevailing notions about the requisite features of a KH domain and raise the possibility that there may be more functional KH domains in the proteome than previously appreciated.
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