Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on December 3, 2004
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
279/49/50654    most recent
M407657200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Martins, A.
Right arrow Articles by Shuman, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Martins, A.
Right arrow Articles by Shuman, S.
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?

Papers In Press, published online ahead of print August 28, 2004
J. Biol. Chem, 10.1074/jbc.M407657200
Submitted on July 8, 2004
Revised on August 19, 2004
Accepted on August 27, 2004

An RNA Ligase from Deinococcus radiodurans

Alexandra Martins and Stewart Shuman

Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10021

Corresponding Author: s-shuman{at}ski.mskcc.org

Although DNA repair pathways have been the focus of much attention, there is an emerging appreciation that distinct pathways exist to maintain or manipulate RNA structure in response to breakage events. Here we identify an RNA ligase (DraRnl) from the radiation-resistant bacterium Deinococcus radiodurans. DraRnl seals 3’-OH/5’-PO4 RNA nicks in either a duplex RNA or an RNA:DNA hybrid, but cannot seal 3’-OH/5’-PO4 DNA nicks. The specificity of DraRnl arises from a requirement for RNA on the 3’-OH side of the nick. DraRnl is a 342–aa monomeric protein with a distinctive structure composed of a C-terminal adenylyltransferase domain linked to an N-terminal module that resembles the OB-fold of phenylalanyl-tRNA synthetases. RNA sealing activity was abolished by mutation of the predicted lysine adenylylation site (Lys165) in the C-terminal domain and was reduced by an order of magnitude by deletion of the N-terminal OB module. Our findings highlight the existence of an RNA repair capacity in bacteria and support the hypothesis that contemporary DNA ligases, RNA ligases, and RNA capping enzymes evolved by fusion of ancillary effector domains to an ancestral catalytic module involved in RNA repair.


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
 J. Biol. Chem.Home page
S. Shuman
DNA Ligases: Progress and Prospects
J. Biol. Chem., June 26, 2009; 284(26): 17365 - 17369.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
C. Torchia, Y. Takagi, and C. K. Ho
Archaeal RNA ligase is a homodimeric protein that catalyzes intramolecular ligation of single-stranded RNA and DNA
Nucleic Acids Res., November 1, 2008; 36(19): 6218 - 6227.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
N. Keppetipola, J. Nandakumar, and S. Shuman
Reprogramming the tRNA-splicing activity of a bacterial RNA repair enzyme
Nucleic Acids Res., June 28, 2007; 35(11): 3624 - 3630.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
A. Raymond and S. Shuman
Deinococcus radiodurans RNA ligase exemplifies a novel ligase clade with a distinctive N-terminal module that is important for 5'-PO4 nick sealing and ligase adenylylation but dispensable for phosphodiester formation at an adenylylated nick
Nucleic Acids Res., February 16, 2007; 35(3): 839 - 849.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Kiyonari, K. Takayama, H. Nishida, and Y. Ishino
Identification of a Novel Binding Motif in Pyrococcus furiosus DNA Ligase for the Functional Interaction with Proliferating Cell Nuclear Antigen
J. Biol. Chem., September 22, 2006; 281(38): 28023 - 28032.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
A. MARTINS and S. SHUMAN
An end-healing enzyme from Clostridium thermocellum with 5' kinase, 2',3' phosphatase, and adenylyltransferase activities
RNA, August 1, 2005; 11(8): 1271 - 1280.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Nandakumar and S. Shuman
Dual Mechanisms whereby a Broken RNA End Assists the Catalysis of Its Repair by T4 RNA Ligase 2
J. Biol. Chem., June 24, 2005; 280(25): 23484 - 23489.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Blondal, S. Hjorleifsdottir, A. Aevarsson, O. H. Fridjonsson, S. Skirnisdottir, J. O. Wheat, A. G. Hermannsdottir, G. O. Hreggvidsson, A. V. Smith, and J. K. Kristjansson
Characterization of a 5'-Polynucleotide Kinase/3'-Phosphatase from Bacteriophage RM378
J. Biol. Chem., February 18, 2005; 280(7): 5188 - 5194.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
T. Blondal, A. Thorisdottir, U. Unnsteinsdottir, S. Hjorleifsdottir, A. Ævarsson, S. Ernstsson, O. H. Fridjonsson, S. Skirnisdottir, J. O. Wheat, A. G. Hermannsdottir, et al.
Isolation and characterization of a thermostable RNA ligase 1 from a Thermus scotoductus bacteriophage TS2126 with good single-stranded DNA ligation properties
Nucleic Acids Res., January 7, 2005; 33(1): 135 - 142.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement