A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization [electronic resource].
- Published
- Washington, D.C. : United States. Dept. of Energy. Office of Basic Energy Sciences, 2014.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy - Physical Description
- pages 18,554-18,559 : digital, PDF file
- Additional Creators
- Yale University, United States. Department of Energy. Office of Basic Energy Sciences, National Institutes of Health (U.S.), and United States. Department of Energy. Office of Scientific and Technical Information
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- Restrictions on Access
- Free-to-read Unrestricted online access
- Summary
- Pumilio/feminization of XX and XO animals (fem)-3 mRNA-binding factor (PUF) proteins bind sequence specifically to mRNA targets using a single-stranded RNA-binding domain comprising eight Pumilio (PUM) repeats. PUM repeats have now been identified in proteins that function in pre-rRNA processing, including human Puf-A and yeast Puf6. This is a role not previously ascribed to PUF proteins. In this paper we present crystal structures of human Puf-A that reveal a class of nucleic acid-binding proteins with 11 PUM repeats arranged in an āLā-like shape. In contrast to classical PUF proteins, Puf-A forms sequence-independent interactions with DNA or RNA, mediated by conserved basic residues. We demonstrate that equivalent basic residues in yeast Puf6 are important for RNA binding, pre-rRNA processing, and mRNA localization. Finally, PUM repeats can be assembled into alternative folds that bind to structured nucleic acids in addition to forming canonical eight-repeat crescent-shaped RNA-binding domains found in classical PUF proteins.
- Report Numbers
- E 1.99:1170010
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- Other Subject(s)
- Note
- Published through SciTech Connect.
12/15/2014.
Proceedings of the National Academy of Sciences of the United States of America 111 52 ISSN 0027-8424 AM
Chen Qiu; Kathleen L. McCann; Robert N. Wine; Susan J. Baserga; Traci M. Tanaka Hall. - Funding Information
- AC02-05CH11231
W-31-109-Eng-38
GM52581
View MARC record | catkey: 23493913