Difference between revisions of "DnaA"

From SubtiWiki
Jump to: navigation, search
(→‎Original publications)
Line 160: Line 160:
 
<pubmed> 16120674, </pubmed>
 
<pubmed> 16120674, </pubmed>
 
==Original publications==
 
==Original publications==
−
'''Additional publications:''' {{PubMed|22396664,21911367}}
+
<pubmed>18854156,19011033, 11222620,14651647,17140409 10844689 ,11222620 12060778 16461910 2987848 2168872 11207367, 19737352 19081080 17932079 19968790 19682252 20511500 21097613 21239581 21895792 22286949 22821970 23909787 22396664,21911367</pubmed>
−
<pubmed>18854156,19011033, 11222620,14651647,17140409 10844689 ,11222620 12060778 16461910 2987848 2168872 11207367, 19737352 19081080 17932079 19968790 19682252 20511500 21097613 21239581 21895792 22286949 22821970</pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:19, 8 August 2013

  • Description: AAA+ ATPase, replication initiation protein

Gene name dnaA
Synonyms dnaH, dnaJ, dnaK
Essential yes PubMed
Product replication initiation protein
Function DNA replication
Gene expression levels in SubtiExpress: dnaA
Interactions involving this protein in SubtInteract: DnaA
MW, pI 50 kDa, 6.035
Gene length, protein length 1338 bp, 446 aa
Immediate neighbours rpmH, dnaN
Sequences Protein DNA DNA_with_flanks
Genetic context
DnaA dnaN yaaA recF yaaB gyrB context.png
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DnaA expression.png















Categories containing this gene/protein

DNA replication, essential genes

This gene is a member of the following regulons

Spo0A regulon

The DnaA regulon

The gene

Basic information

  • Locus tag: BSU00010

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:
    • binds multiple regions in the oriC region, required for recruitment of proteins needed to load the replicative helicase DnaC
  • Protein family: dnaA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: AAA+ domain
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
    • SirA displaces DnaA from the replication origin PubMed
    • YabA inhibits co-operative binding of DnaA to the oriC DNA PubMed
    • DnaA helix formation (and thus replication initiation) is inhibited by the interaction of Soj with the AAA+ domain of DnaA PubMed
    • interaction with DnaD inhibits the ability of DnaA to cooperatively bind to DNA PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

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


The DnaA regulon

Original publications

Graham Scholefield, Heath Murray
YabA and DnaD inhibit helix assembly of the DNA replication initiation protein DnaA.
Mol Microbiol: 2013, 90(1);147-59
[PubMed:23909787] [WorldCat.org] [DOI] (I p)

Carla Y Bonilla, Alan D Grossman
The primosomal protein DnaD inhibits cooperative DNA binding by the replication initiator DnaA in Bacillus subtilis.
J Bacteriol: 2012, 194(18);5110-7
[PubMed:22821970] [WorldCat.org] [DOI] (I p)

Norbert S Hill, Ryosuke Kadoya, Dhruba K Chattoraj, Petra Anne Levin
Cell size and the initiation of DNA replication in bacteria.
PLoS Genet: 2012, 8(3);e1002549
[PubMed:22396664] [WorldCat.org] [DOI] (I p)

Graham Scholefield, Jeff Errington, Heath Murray
Soj/ParA stalls DNA replication by inhibiting helix formation of the initiator protein DnaA.
EMBO J: 2012, 31(6);1542-55
[PubMed:22286949] [WorldCat.org] [DOI] (I p)

Hajime Okumura, Mika Yoshimura, Mikako Ueki, Taku Oshima, Naotake Ogasawara, Shu Ishikawa
Regulation of chromosomal replication initiation by oriC-proximal DnaA-box clusters in Bacillus subtilis.
Nucleic Acids Res: 2012, 40(1);220-34
[PubMed:21911367] [WorldCat.org] [DOI] (I p)

Houra Merrikh, Alan D Grossman
Control of the replication initiator DnaA by an anti-cooperativity factor.
Mol Microbiol: 2011, 82(2);434-46
[PubMed:21895792] [WorldCat.org] [DOI] (I p)

Lilah Rahn-Lee, Houra Merrikh, Alan D Grossman, Richard Losick
The sporulation protein SirA inhibits the binding of DnaA to the origin of replication by contacting a patch of clustered amino acids.
J Bacteriol: 2011, 193(6);1302-7
[PubMed:21239581] [WorldCat.org] [DOI] (I p)

Wiep Klaas Smits, Houra Merrikh, Carla Yaneth Bonilla, Alan D Grossman
Primosomal proteins DnaD and DnaB are recruited to chromosomal regions bound by DnaA in Bacillus subtilis.
J Bacteriol: 2011, 193(3);640-8
[PubMed:21097613] [WorldCat.org] [DOI] (I p)

Sharon E Hoover, Weihong Xu, Wenzhong Xiao, William F Burkholder
Changes in DnaA-dependent gene expression contribute to the transcriptional and developmental response of Bacillus subtilis to manganese limitation in Luria-Bertani medium.
J Bacteriol: 2010, 192(15);3915-24
[PubMed:20511500] [WorldCat.org] [DOI] (I p)

Wiep Klaas Smits, Alexi I Goranov, Alan D Grossman
Ordered association of helicase loader proteins with the Bacillus subtilis origin of replication in vivo.
Mol Microbiol: 2010, 75(2);452-61
[PubMed:19968790] [WorldCat.org] [DOI] (I p)

Alexi I Goranov, Adam M Breier, Houra Merrikh, Alan D Grossman
YabA of Bacillus subtilis controls DnaA-mediated replication initiation but not the transcriptional response to replication stress.
Mol Microbiol: 2009, 74(2);454-66
[PubMed:19737352] [WorldCat.org] [DOI] (I p)

Jennifer K Wagner, Kathleen A Marquis, David Z Rudner
SirA enforces diploidy by inhibiting the replication initiator DnaA during spore formation in Bacillus subtilis.
Mol Microbiol: 2009, 73(5);963-74
[PubMed:19682252] [WorldCat.org] [DOI] (I p)

Clarisse Defeu Soufo, Hervé Joël Defeu Soufo, Marie-Françoise Noirot-Gros, Astrid Steindorf, Philippe Noirot, Peter L Graumann
Cell-cycle-dependent spatial sequestration of the DnaA replication initiator protein in Bacillus subtilis.
Dev Cell: 2008, 15(6);935-41
[PubMed:19081080] [WorldCat.org] [DOI] (I p)

Adam M Breier, Alan D Grossman
Dynamic association of the replication initiator and transcription factor DnaA with the Bacillus subtilis chromosome during replication stress.
J Bacteriol: 2009, 191(2);486-93
[PubMed:19011033] [WorldCat.org] [DOI] (I p)

Heath Murray, Jeff Errington
Dynamic control of the DNA replication initiation protein DnaA by Soj/ParA.
Cell: 2008, 135(1);74-84
[PubMed:18854156] [WorldCat.org] [DOI] (I p)

Shu Ishikawa, Yoshitoshi Ogura, Mika Yoshimura, Hajime Okumura, Eunha Cho, Yoshikazu Kawai, Ken Kurokawa, Taku Oshima, Naotake Ogasawara
Distribution of stable DnaA-binding sites on the Bacillus subtilis genome detected using a modified ChIP-chip method.
DNA Res: 2007, 14(4);155-68
[PubMed:17932079] [WorldCat.org] [DOI] (P p)

Melanie B Berkmen, Alan D Grossman
Subcellular positioning of the origin region of the Bacillus subtilis chromosome is independent of sequences within oriC, the site of replication initiation, and the replication initiator DnaA.
Mol Microbiol: 2007, 63(1);150-65
[PubMed:17140409] [WorldCat.org] [DOI] (P p)

Marie-Françoise Noirot-Gros, M Velten, M Yoshimura, S McGovern, T Morimoto, S D Ehrlich, N Ogasawara, P Polard, Philippe Noirot
Functional dissection of YabA, a negative regulator of DNA replication initiation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2006, 103(7);2368-73
[PubMed:16461910] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Marie-Françoise Noirot-Gros, Etienne Dervyn, Ling Juan Wu, Peggy Mervelet, Jeffery Errington, S Dusko Ehrlich, Philippe Noirot
An expanded view of bacterial DNA replication.
Proc Natl Acad Sci U S A: 2002, 99(12);8342-7
[PubMed:12060778] [WorldCat.org] [DOI] (P p)

D Ishigo-Oka, N Ogasawara, S Moriya
DnaD protein of Bacillus subtilis interacts with DnaA, the initiator protein of replication.
J Bacteriol: 2001, 183(6);2148-50
[PubMed:11222620] [WorldCat.org] [DOI] (P p)

W F Burkholder, I Kurtser, A D Grossman
Replication initiation proteins regulate a developmental checkpoint in Bacillus subtilis.
Cell: 2001, 104(2);269-79
[PubMed:11207367] [WorldCat.org] [DOI] (P p)

Y Imai, N Ogasawara, D Ishigo-Oka, R Kadoya, T Daito, S Moriya
Subcellular localization of Dna-initiation proteins of Bacillus subtilis: evidence that chromosome replication begins at either edge of the nucleoids.
Mol Microbiol: 2000, 36(5);1037-48
[PubMed:10844689] [WorldCat.org] [DOI] (P p)

T Fukuoka, S Moriya, H Yoshikawa, N Ogasawara
Purification and characterization of an initiation protein for chromosomal replication, DnaA, in Bacillus subtilis.
J Biochem: 1990, 107(5);732-9
[PubMed:2168872] [WorldCat.org] [DOI] (P p)

N Ogasawara, S Moriya, H Yoshikawa
Structure and function of the region of the replication origin of the Bacillus subtilis chromosome. IV. Transcription of the oriC region and expression of DNA gyrase genes and other open reading frames.
Nucleic Acids Res: 1985, 13(7);2267-79
[PubMed:2987848] [WorldCat.org] [DOI] (P p)

Retrieved from "https://subtiwiki.uni-goettingen.de/wiki//index.php?title=DnaA&oldid=193364"