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Proc Natl Acad Sci U S A. 2014 Dec 30;111(52):18554-9. doi: 10.1073/pnas.1407634112. Epub 2014 Dec 15.

A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization.

Author information

1
Epigenetics and Stem Cell Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709; and.
2
Departments of Genetics.
3
Departments of Genetics, Molecular Biophysics and Biochemistry, and Therapeutic Radiology, Yale University School of Medicine, New Haven, CT 06520 hall4@niehs.nih.gov susan.baserga@yale.edu.
4
Epigenetics and Stem Cell Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709; and hall4@niehs.nih.gov susan.baserga@yale.edu.

Abstract

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. Here we present crystal structures of human Puf-A that reveal a class of nucleic acid-binding proteins with 11 PUM repeats arranged in an "L"-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. Thus, 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.

KEYWORDS:

Puf-A; Puf6; crystal structure; mRNA localization; ribosome biogenesis

PMID:
25512524
PMCID:
PMC4284587
DOI:
10.1073/pnas.1407634112
[Indexed for MEDLINE]
Free PMC Article
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