Document Detail


Binding mechanism of metal⋅NTP substrates and stringent-response alarmones to bacterial DnaG-type primases.
MedLine Citation:
PMID:  22795082     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Primases are DNA-dependent RNA polymerases found in all cellular organisms. In bacteria, primer synthesis is carried out by DnaG, an essential enzyme that serves as a key component of DNA replication initiation, progression, and restart. How DnaG associates with nucleotide substrates and how certain naturally prevalent nucleotide analogs impair DnaG function are unknown. We have examined one of the earliest stages in primer synthesis and its control by solving crystal structures of the S. aureus DnaG catalytic core bound to metal ion cofactors and either individual nucleoside triphosphates or the nucleotidyl alarmones, pppGpp and ppGpp. These structures, together with both biochemical analyses and comparative studies of enzymes that use the same catalytic fold as DnaG, pinpoint the predominant nucleotide-binding site of DnaG and explain how the induction of the stringent response in bacteria interferes with primer synthesis.
Authors:
Richard U Rymer; Francisco A Solorio; Ashley K Tehranchi; Clement Chu; Jacob E Corn; James L Keck; Jue D Wang; James M Berger
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-07-12
Journal Detail:
Title:  Structure (London, England : 1993)     Volume:  20     ISSN:  1878-4186     ISO Abbreviation:  Structure     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-09-10     Completed Date:  2013-01-22     Revised Date:  2013-09-10    
Medline Journal Info:
Nlm Unique ID:  101087697     Medline TA:  Structure     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1478-89     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Ltd. All rights reserved.
Affiliation:
California Institute for Quantitative Biosciences, 374D Stanley Hall #3220, University of California, Berkeley, Berkeley, CA 94720-3220, USA.
Data Bank Information
Bank Name/Acc. No.:
PDB/4EDG;  4EDK;  4EDT;  4EDV;  4EE1
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / chemistry*
Catalytic Domain
Coenzymes / chemistry
Conserved Sequence
Coordination Complexes / chemistry
Crystallography, X-Ray
DNA Primase / chemistry*
Deoxyribonucleotides / chemistry*
Guanosine Pentaphosphate / chemistry*
Guanosine Tetraphosphate / chemistry*
Manganese / chemistry
Models, Molecular
Protein Binding
Protein Structure, Secondary
Staphylococcus aureus / enzymology*
Stress, Physiological
Grant Support
ID/Acronym/Agency:
GM071747/GM/NIGMS NIH HHS; GM084003/GM/NIGMS NIH HHS; R01 GM071747/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Coenzymes; 0/Coordination Complexes; 0/Deoxyribonucleotides; 33503-72-9/Guanosine Tetraphosphate; 38918-96-6/Guanosine Pentaphosphate; 7439-96-5/Manganese; EC 2.7.7.-/DNA Primase
Comments/Corrections
Comment In:
Structure. 2012 Sep 5;20(9):1447-8   [PMID:  22958638 ]

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


Previous Document:  A position paper on standardizing the nonneoplastic kidney biopsy report.
Next Document:  Structure of a Bacteriophytochrome and Light-Stimulated Protomer Swapping with a Gene Repressor.