Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Published online before print February 6, 2004, 10.1110/ps.03477004
Protein Science (2004), 13:668-677. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
ps.03477004v1
13/3/668    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Harlow, L. S.
Right arrow Articles by Larsen, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Harlow, L. S.
Right arrow Articles by Larsen, S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding

Lene S. Harlow1,3, Anders Kadziola2,3, Kaj Frank Jensen1 and Sine Larsen2

1 Department of Biological Chemistry, Institute of Molecular Biology, and
2 Centre for Crystallographic Studies, Department of Chemistry, University of Copenhagen, Copenhagen, Denmark

(RECEIVED October 8, 2003; FINAL REVISION November 28, 2003; ACCEPTED December 1, 2003)



Abstract

RNase PH is a member of the family of phosphorolytic 3' -> 5' exoribonucleases that also includes polynucleotide phosphorylase (PNPase). RNase PH is involved in the maturation of tRNA precursors and especially important for removal of nucleotide residues near the CCA acceptor end of the mature tRNAs. Wild-type and triple mutant R68Q-R73Q-R76Q RNase PH from Bacillus subtilis have been crystallized and the structures determined by X-ray diffraction to medium resolution. Wild-type and triple mutant RNase PH crystallize as a hexamer and dimer, respectively. The structures contain a rare left-handed {beta}{alpha}{beta}-motif in the N-terminal portion of the protein. This motif has also been identified in other enzymes involved in RNA metabolism. The RNase PH structure and active site can, despite low sequence similarity, be overlayed with the N-terminal core of the structure and active site of Streptomyces antibioticus PNPase. The surface of the RNase PH dimer fit the shape of a tRNA molecule.

Keywords: crystal structure; maturation of tRNA; ribonuclease; RNase PH; tRNA precursor

Abbreviations: RNase, ribonuclease • PNPase, polynucleotide phosphorylase • Tris, 2-amino-2-hydroxymethyl-1,3-propanediol • MES, 2-[N-morpholino]ethanesulfonic acid • PEG, polyethylene glucol

Reprint requests to: Anders Kadziola, Centre for Crystallographic Studies, Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark; e-mail: anders{at}ccs.ki.ku.dk; fax: +45-35-32-02-99.

3 These authors have contributed equally to this work.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03477004.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
C. R. R. Ramos, C. L. P. Oliveira, I. L. Torriani, and C. C. Oliveira
The Pyrococcus Exosome Complex: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION
J. Biol. Chem., March 10, 2006; 281(10): 6751 - 6759.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
U. Z. Littauer
From Polynucleotide Phosphorylase to Neurobiology
J. Biol. Chem., November 25, 2005; 280(47): 38889 - 38897.
[Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
T. Wen, I. A. Oussenko, O. Pellegrini, D. H. Bechhofer, and C. Condon
Ribonuclease PH plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors in Bacillus subtilis
Nucleic Acids Res., June 27, 2005; 33(11): 3636 - 3643.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by The Protein Society.