The Thermus thermophilus DEAD-box protein Hera is a general RNA binding protein and plays a key role in tRNA metabolism.

RNA
Pascal DonsbachDagmar Klostermeier

Abstract

RNA helicases catalyze the ATP-dependent destabilization of RNA duplexes. DEAD-box helicases share a helicase core that mediates ATP binding and hydrolysis, RNA binding and unwinding. Most members of this family contain domains flanking the core that can confer RNA substrate specificity and guide the helicase to a specific RNA. However, the in vivo RNA substrates of most helicases are currently not defined. The DEAD-box helicase Hera from Thermus thermophilus contains a helicase core, followed by a dimerization domain and an RNA binding domain that folds into an RNA recognition motif (RRM). The RRM mediates high affinity binding to an RNA hairpin, and an adjacent duplex is then unwound by the helicase core. Hera is a cold-shock protein, and has been suggested to act as an RNA chaperone under cold-shock conditions. Using crosslinking immunoprecipitation of Hera/RNA complexes and sequencing, we show that Hera binds to a large fraction of T. thermophilus RNAs under normal-growth and cold-shock conditions without a strong sequence preference, in agreement with a structure-specific recognition of RNAs and a general function in RNA metabolism. Under cold-shock conditions, Hera is recruited to RNAs with high propensities to form stabl...Continue Reading

References

Jan 1, 1989·Methods in Enzymology·M Zuker
Jan 9, 1996·Proceedings of the National Academy of Sciences of the United States of America·P G JonesM Inouye
Mar 1, 1997·Journal of Bacteriology·J J DallugeJ A McCloskey
Mar 12, 1999·Journal of Bacteriology·D ChamotG W Owttrim
Apr 27, 1999·The International Journal of Biochemistry & Cell Biology·J LuM C Ganoza
Jun 11, 1999·Current Opinion in Structural Biology·D K Treiber, J R Williamson
Oct 20, 1999·Journal of Molecular Biology·G E PughF V Fuller-Pace
May 29, 2000·Trends in Genetics : TIG·P RiceA Bleasby
Jan 4, 2001·Extremophiles : Life Under Extreme Conditions·R CavicchioliP M Curmi
Sep 11, 2002·Progress in Nucleic Acid Research and Molecular Biology·George W RogersWilliam C Merrick
Dec 4, 2002·Journal of Molecular Biology·Karl KossenOlke C Uhlenbeck
Jun 26, 2003·Nucleic Acids Research·Michael Zuker
Mar 3, 2004·Nature Reviews. Molecular Cell Biology·Sanda Rocak, Patrick Linder
Apr 6, 2004·Nature Biotechnology·Anke HenneHans-Joachim Fritz
Jun 3, 2004·Nucleic Acids Research·Fedor V Karginov, Olke C Uhlenbeck
May 26, 2005·Protein Expression and Purification·F William Studier
Aug 25, 2005·The Journal of Biological Chemistry·Fedor V KarginovOlke C Uhlenbeck
Dec 1, 2005·The Journal of Biological Chemistry·Naoki ShigiKimitsuna Watanabe
Apr 25, 2006·Cell·Toru SengokuShigeyuki Yokoyama
Aug 8, 2006·Journal of Molecular Biology·Markus G RudolphDagmar Klostermeier
Nov 1, 2006·Proceedings of the National Academy of Sciences of the United States of America·Pilar TijerinaRick Russell
Jan 10, 2009·Nature Protocols·Da Wei HuangRichard A Lempicki
Mar 4, 2009·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Markus G RudolphDagmar Klostermeier
Mar 27, 2009·The EMBO Journal·Sarin ChimnaronkIsao Tanaka
May 22, 2009·Nucleic Acids Research·Timothy L BaileyWilliam S Noble
Sep 8, 2009·Nucleic Acids Research·Lisa M Sharpe EllesOlke C Uhlenbeck

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