Difference between revisions of "DnaE"

From SubtiWiki
Jump to: navigation, search
(Original publications)
Line 108: Line 108:
 
=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''Structure:'''
 +
** [http://www.pdb.org/pdb/explore/explore.do?structureId=3e0d 3E0D] (from ''Thermus aquaticus'', 39% identity) {{PubMed|18691598}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34623 O34623]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34623 O34623]
Line 156: Line 157:
 
<pubmed> 22933559 </pubmed>
 
<pubmed> 22933559 </pubmed>
 
== Original publications ==
 
== Original publications ==
<pubmed>,11721055,14593098,16267290, 20122408 23563155 23017159,21958350,23268446 24062730 24106089</pubmed>
+
<pubmed>,11721055,14593098,16267290, 20122408 23563155 23017159,21958350,23268446 24062730 24106089 18691598</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:16, 17 November 2013

  • Description: DNA polymerase III (alpha subunit), part of the replisome

Gene name dnaE
Synonyms
Essential yes PubMed
Product DNA polymerase III (alpha subunit)
Function DNA replication
Gene expression levels in SubtiExpress: dnaE
Interactions involving this protein in SubtInteract: DnaE
MW, pI 125 kDa, 6.02
Gene length, protein length 3345 bp, 1115 aa
Immediate neighbours ytsJ, ytrH
Sequences Protein DNA DNA_with_flanks
Genetic context
DnaE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DnaE expression.png















Categories containing this gene/protein

DNA replication, essential genes

This gene is a member of the following regulons

LexA regulon

The gene

Basic information

  • Locus tag: BSU29230

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1) (according to Swiss-Prot)
    • required for bacteriophage SPP1 replication PubMed
  • Protein family: DnaE subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • forms foci, the foci dissappear after the formation of DNA mismatches in a MutS-dependent manner or after DNA replication arrest PubMed
    • cytoplasm (according to Swiss-Prot)

Database entries

  • Structure:
    • 3E0D (from Thermus aquaticus, 39% identity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Kestutis Timinskas, Monika Balvočiūtė, Albertas Timinskas, Česlovas Venclovas
Comprehensive analysis of DNA polymerase III α subunits and their homologs in bacterial genomes.
Nucleic Acids Res: 2014, 42(3);1393-413
[PubMed:24106089] [WorldCat.org] [DOI] (I p)

Motohiro Akashi, Hirofumi Yoshikawa
Relevance of GC content to the conservation of DNA polymerase III/mismatch repair system in Gram-positive bacteria.
Front Microbiol: 2013, 4;266
[PubMed:24062730] [WorldCat.org] [DOI] (P e)

Olivier Rannou, Emmanuelle Le Chatelier, Marilynn A Larson, Hamid Nouri, Bérengère Dalmais, Charles Laughton, Laurent Jannière, Panos Soultanas
Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis.
Nucleic Acids Res: 2013, 41(10);5303-20
[PubMed:23563155] [WorldCat.org] [DOI] (I p)

Elena M Seco, John C Zinder, Carol M Manhart, Ambra Lo Piano, Charles S McHenry, Silvia Ayora
Bacteriophage SPP1 DNA replication strategies promote viral and disable host replication in vitro.
Nucleic Acids Res: 2013, 41(3);1711-21
[PubMed:23268446] [WorldCat.org] [DOI] (I p)

Marjorie H Barnes, Michelle M Butler, George E Wright, Neal C Brown
Antimicrobials targeted to the replication-specific DNA polymerases of gram-positive bacteria: target potential of dnaE.
Infect Disord Drug Targets: 2012, 12(5);327-31
[PubMed:23017159] [WorldCat.org] [DOI] (I p)

Andrew D Klocko, Jeremy W Schroeder, Brian W Walsh, Justin S Lenhart, Margery L Evans, Lyle A Simmons
Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork.
Mol Microbiol: 2011, 82(3);648-63
[PubMed:21958350] [WorldCat.org] [DOI] (I p)

Glenn M Sanders, H Garry Dallmann, Charles S McHenry
Reconstitution of the B. subtilis replisome with 13 proteins including two distinct replicases.
Mol Cell: 2010, 37(2);273-81
[PubMed:20122408] [WorldCat.org] [DOI] (I p)

Richard A Wing, Scott Bailey, Thomas A Steitz
Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit.
J Mol Biol: 2008, 382(4);859-69
[PubMed:18691598] [WorldCat.org] [DOI] (I p)

Nora Au, Elke Kuester-Schoeck, Veena Mandava, Laura E Bothwell, Susan P Canny, Karen Chachu, Sierra A Colavito, Shakierah N Fuller, Eli S Groban, Laura A Hensley, Theresa C O'Brien, Amish Shah, Jessica T Tierney, Louise L Tomm, Thomas M O'Gara, Alexi I Goranov, Alan D Grossman, Charles M Lovett
Genetic composition of the Bacillus subtilis SOS system.
J Bacteriol: 2005, 187(22);7655-66
[PubMed:16267290] [WorldCat.org] [DOI] (P p)

Emmanuelle Le Chatelier, Olivier J Bécherel, Emmanuelle d'Alençon, Danielle Canceill, S Dusko Ehrlich, Robert P P Fuchs, Laurent Jannière
Involvement of DnaE, the second replicative DNA polymerase from Bacillus subtilis, in DNA mutagenesis.
J Biol Chem: 2004, 279(3);1757-67
[PubMed:14593098] [WorldCat.org] [DOI] (P p)

E Dervyn, C Suski, R Daniel, C Bruand, J Chapuis, J Errington, L Jannière, S D Ehrlich
Two essential DNA polymerases at the bacterial replication fork.
Science: 2001, 294(5547);1716-9
[PubMed:11721055] [WorldCat.org] [DOI] (P p)