Yeast Nab3 Protein Contains a Self-assembly Domain Found in Human Heterogeneous Nuclear Ribonucleoprotein-C (hnRNP-C) That Is Necessary for Transcription Termination

• Type of Material: Article
• Authors: Travis J. Loya, Emory University; Thomas W. O'Rourke, Emory University; Daniel Reines, Emory University
• Language: English
• Date: 2013-01-25
• Publisher: American Society for Biochemistry and Molecular Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
• Final Published Version (URL): http://www.jbc.org/content/288/4/2111
• Title of Journal or Parent Work: Journal of Biological Chemistry
• ISSN: 0021-9258
• Volume: 288
• Issue: 4
• Start Page: 2111
• End Page: 2117
• Grant/Funding Information: This work was supported, in whole or in part, by National Institutes of Health Grant GM46331.
• Keywords: Transcription Termination; Polyglutamine; RNA-binding Protein; Nab3; RNA-Protein Interaction; Yeast; hnRNP
• Research Categories: Chemistry, Biochemistry

Abstract

Background: Termination factor Nab3 binds RNA, but its function and structure are poorly understood. Results: The carboxyl terminus of Nab3 functions as a self-assembly region important for termination. Conclusion: Nab3 resembles hnRNP-C in this new function, indicating that it is related to mammalian RNA-packaging proteins. Significance: Nab3 coats RNA to form a higher order assembly due to interactions among RNA, RNA polymerase, and hnRNPs.