JBC Biosymposia, Inc.

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


     


Originally published In Press as doi:10.1074/jbc.M409277200 on December 13, 2004

J. Biol. Chem., Vol. 280, Issue 7, 5503-5509, February 18, 2005
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
280/7/5503    most recent
M409277200v1
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 Jacob, Y.
Right arrow Articles by Williams, K. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jacob, Y.
Right arrow Articles by Williams, K. P.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Function of the SmpB Tail in Transfer-messenger RNA Translation Revealed by a Nucleus-encoded Form*

Yannick Jacob, Stephen M. Sharkady, Kanchan Bhardwaj{ddagger}, Alina Sanda, and Kelly P. Williams§

From the Department of Biology, Indiana University, Bloomington, Indiana 47405

Stalled bacterial ribosomes are freed when they switch to the translation of transfer-messenger RNA (tmRNA). This process requires the tmRNA-binding and ribosome-binding cofactor SmpB, a {beta}-barrel protein with a protruding C-terminal tail of unresolved structure. Some plastid genomes encode tmRNA, but smpB genes have only been reported from bacteria. Here we identify smpB in the nuclear genomes of both a diatom and a red alga encoding a signal for import into the plastid, where mature SmpB could activate tmRNA. Diatom SmpB was active for tmRNA translation with bacterial components in vivo and in vitro, although less so than Escherichia coli SmpB. The tail-truncated diatom SmpB, the hypothetical product of a misspliced mRNA, was inactive in vivo. Tail-truncated E. coli SmpB was likewise inactive for tmRNA translation but was still able to bind ribosomes, and its affinity for tmRNA was only slightly diminished. This work suggests that SmpB is a universal cofactor of tmRNA. It also reveals a tail-dependent role for SmpB in tmRNA translation that supersedes a simple role of linking tmRNA to the ribosome, which the SmpB body alone could provide.


Received for publication, August 12, 2004 , and in revised form, December 9, 2004.

* This study was supported by grants from Le Fond Québécois de la Recherche sur la Nature et les Technologies (to Y. J.) and the National Institutes of Health (to K. P. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} Present address: Dept. of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128.

§ To whom correspondence should be addressed: Dept. of Biology, Indiana University, 1001 E. 3rd St., Bloomington, IN 47405. Tel.: 812-856-5697; Fax: 812-855-6705; E-mail: kellwill{at}indiana.edu.


Add to CiteULike CiteULike   Add to Complore Complore   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
RNAHome page
L. Metzinger, M. Hallier, and B. Felden
The highest affinity binding site of small protein B on transfer messenger RNA is outside the tRNA domain
RNA, September 1, 2008; 14(9): 1761 - 1772.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
D. Kurita, R. Sasaki, A. Muto, and H. Himeno
Interaction of SmpB with ribosome from directed hydroxyl radical probing
Nucleic Acids Res., December 18, 2007; 35(21): 7248 - 7255.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. R. Sundermeier and A. W. Karzai
Functional SmpB-Ribosome Interactions Require tmRNA
J. Biol. Chem., November 30, 2007; 282(48): 34779 - 34786.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
T. Konno, D. Kurita, K. Takada, A. Muto, and H. Himeno
A functional interaction of SmpB with tmRNA for determination of the resuming point of trans-translation
RNA, October 1, 2007; 13(10): 1723 - 1731.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
Y. Bessho, R. Shibata, S.-i. Sekine, K. Murayama, K. Higashijima, C. Hori-Takemoto, M. Shirouzu, S. Kuramitsu, and S. Yokoyama
Structural basis for functional mimicry of long-variable-arm tRNA by transfer-messenger RNA
PNAS, May 15, 2007; 104(20): 8293 - 8298.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
M. Saguy, R. Gillet, P. Skorski, S. Hermann-Le Denmat, and B. Felden
Ribosomal protein S1 influences trans-translation in vitro and in vivo
Nucleic Acids Res., April 1, 2007; 35(7): 2368 - 2376.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
M. Hallier, J. Desreac, and B. Felden
Small protein B interacts with the large and the small subunits of a stalled ribosome during trans-translation.
Nucleic Acids Res., January 1, 2006; 34(6): 1935 - 1943.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
E. S. Andersen, M. A. Rosenblad, N. Larsen, J. C. Westergaard, J. Burks, I. K. Wower, J. Wower, J. Gorodkin, T. Samuelsson, and C. Zwieb
The tmRDB and SRPDB resources
Nucleic Acids Res., January 1, 2006; 34(suppl_1): D163 - D168.
[Abstract] [Full Text] [PDF]


Home page
J BiochemHome page
N. Nameki, T. Someya, S. Okano, R. Suemasa, M. Kimoto, K. Hanawa-Suetsugu, T. Terada, M. Shirouzu, I. Hirao, H. Takaku, et al.
Interaction Analysis between tmRNA and SmpB from Thermus thermophilus
J. Biochem., December 1, 2005; 138(6): 729 - 739.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
N. Ivanova, M. Y. Pavlov, E. Bouakaz, M. Ehrenberg, and L. H. Schiavone
Mapping the interaction of SmpB with ribosomes by footprinting of ribosomal RNA
Nucleic Acids Res., June 21, 2005; 33(11): 3529 - 3539.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.