Document Detail


The C-terminal domain is sufficient for endonuclease activity of Neisseria gonorrhoeae MutL.
MedLine Citation:
PMID:  19656086     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The mutL gene of Neisseria gonorrhoeae has been cloned and the gene product purified. We have found that the homodimeric N. gonorrhoeae MutL (NgoL) protein displays an endonuclease activity that incises covalently closed circular DNA in the presence of Mn(2+), Mg(2+) or Ca(2+) ions, unlike human MutLalpha which shows endonuclease activity only in the presence of Mn(2+). We report in the present paper that the C-terminal domain of N. gonorrhoeae MutL (NgoL-CTD) consisting of amino acids 460-658 exhibits Mn(2+)-dependent endonuclease activity. Sedimentation velocity, sedimentation equilibrium and dynamic light scattering experiments show NgoL-CTD to be a dimer. The probable endonucleolytic active site is localized to a metal-binding motif, DMHAX2EX4E, and the nicking endonuclease activity is dependent on the integrity of this motif. By in vitro comparison of wild-type and a mutant NgoL-CTD protein, we show that the latter protein exhibits highly reduced endonuclease activity. We therefore suggest that the mode of excision initiation in DNA mismatch repair may be different in organisms that lack MutH protein, but have MutL proteins that harbour the D[M/Q]HAX2EX4E motif.
Authors:
Viswanadham Duppatla; Chiranjeevi Bodda; Claus Urbanke; Peter Friedhoff; Desirazu N Rao
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-09-25
Journal Detail:
Title:  The Biochemical journal     Volume:  423     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2009 Oct 
Date Detail:
Created Date:  2009-09-23     Completed Date:  2009-10-13     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  265-77     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Indian Institute of Science, Bangalore, India.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / analysis,  genetics,  metabolism,  physiology
Amino Acid Sequence
Bacterial Proteins / chemistry,  genetics,  metabolism,  physiology
DNA / metabolism
DNA Repair Enzymes / chemistry,  genetics,  metabolism,  physiology
Endonucleases / chemistry*,  genetics,  metabolism*,  physiology
Escherichia coli Proteins / analysis,  genetics
Genetic Complementation Test
Molecular Sequence Data
Neisseria gonorrhoeae / enzymology*,  genetics
Phenotype
Protein Binding
Protein Multimerization / physiology
Protein Structure, Tertiary / physiology
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/MutL protein, E coli; 9007-49-2/DNA; EC 3.1.-/Endonucleases; EC 3.6.1.-/Adenosine Triphosphatases; EC 6.5.1.-/DNA Repair Enzymes

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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