Rv2592c - holliday junction DNA helicase ruvB


Protein Domains

Gene Information
LocusRv2592c
SymbolruvB
Gene Nameholliday junction DNA helicase ruvB
Location2923199 - 2924233 (-)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:1035 bp
Protein:345 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number712
Related GenesAcel_1343 BL0729 CE1773 cg1869 DIP1375 jk1054 MAP1038 MAV_3473 Mkms_2314 ML0483 Mmcs_2267 MSMEG_2945 MT2669 MUL_1716 Mvan_2575 nfa36950 PPA1160 SAV6835
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv2592c
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Structural Analysis
D. Schnappinger,S. Ehrt,MI. Voskuil,Y. Liu,JA. Mangan,IM. Monahan,G. Dolganov,B. Efron,PD. Butcher,C. Nathan,GK. Schoolnik Transcriptional Adaptation of Mycobacterium tuberculosis within Macrophages: Insights into the Phagosomal Environment. J. Exp. Med. 2003
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Structural Analysis
authors,P. McGlynn,AA. Mahdi,RG. Lloyd Characterisation of the catalytically active form of RecG helicase. Nucleic Acids Res. 2000
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Structural Analysis
authors,ME. Robu,RB. Inman,MM. Cox Situational repair of replication forks: roles of RecG and RecA proteins. J. Biol. Chem. 2004
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Structural Analysis
authors,AV. Gregg,P. McGlynn,RP. Jaktaji,RG. Lloyd Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities. Mol. Cell 2002
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Structural Analysis
authors,MR. Singleton,S. Scaife,DB. Wigley Structural analysis of DNA replication fork reversal by RecG. Cell 2001
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Structural Analysis
authors,GJ. Sharples,SM. Ingleston,RG. Lloyd Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA. J. Bacteriol. 1999
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Spectrophotometric
D. Schnappinger,S. Ehrt,MI. Voskuil,Y. Liu,JA. Mangan,IM. Monahan,G. Dolganov,B. Efron,PD. Butcher,C. Nathan,GK. Schoolnik Transcriptional Adaptation of Mycobacterium tuberculosis within Macrophages: Insights into the Phagosomal Environment. J. Exp. Med. 2003
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Spectrophotometric
authors,P. McGlynn,AA. Mahdi,RG. Lloyd Characterisation of the catalytically active form of RecG helicase. Nucleic Acids Res. 2000
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Spectrophotometric
authors,ME. Robu,RB. Inman,MM. Cox Situational repair of replication forks: roles of RecG and RecA proteins. J. Biol. Chem. 2004
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Spectrophotometric
authors,AV. Gregg,P. McGlynn,RP. Jaktaji,RG. Lloyd Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities. Mol. Cell 2002
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Spectrophotometric
authors,MR. Singleton,S. Scaife,DB. Wigley Structural analysis of DNA replication fork reversal by RecG. Cell 2001
InteractionPhysicalInteraction Rv2973cactiveshahanup862012-10-05
Spectrophotometric
authors,GJ. Sharples,SM. Ingleston,RG. Lloyd Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA. J. Bacteriol. 1999
InteractionPhysicalInteraction Rv2603cactivesureshks892012-10-05

authors,MY. Galperin,EV. Koonin From complete genome sequence to 'complete' understanding? Trends Biotechnol. 2010
InteractionPhysicalInteraction Rv2603cactivesureshks892012-10-05

authors,H. Liang,L. Li,Z. Dong,MG. Surette,K. Duan The YebC family protein PA0964 negatively regulates the Pseudomonas aeruginosa quinolone signal system and pyocyanin production. J. Bacteriol. 2008
InteractionPhysicalInteraction Rv2594cactiveshahanup862012-10-05
Co-expression (Functional linkage)
PC. Brooks, F. Movahedzadeh et al. Identification of some DNA damage-inducible genes of Mycobacterium tuberculosis: apparent lack of correlation with LexA binding. J. Bacteriol. 2001
InteractionPhysicalInteraction Rv2594cactiveshahanup862012-10-05
Co-expression (Functional linkage)
JR. Prabu, S. Thamotharan et al. Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2006
InteractionPhysicalInteraction Rv2594cactiveshahanup862012-10-05
Co-expression (Functional linkage)
PC. Brooks, F. Movahedzadeh et al. Identification of some DNA damage-inducible genes of Mycobacterium tuberculosis: apparent lack of correlation with LexA binding. J. Bacteriol. 2001
InteractionPhysicalInteraction Rv2594cactiveshahanup862012-10-05
Co-expression (Functional linkage)
JR. Prabu, S. Thamotharan et al. Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2006
InteractionPhysicalInteraction Rv2593cactiveshahanup862012-10-05
Structural Analysis
authors,CV. Privezentzev,A. Keeley,B. Sigala,IR. Tsaneva The role of RuvA octamerization for RuvAB function in vitro and in vivo. J. Biol. Chem. 2005
InteractionPhysicalInteraction Rv2593cactiveshahanup862012-10-05
Structural Analysis
JS. Khanduja, P. Tripathi et al. Mycobacterium tuberculosis RuvA Induces Two Distinct Types of Structural Distortions between the Homologous and Heterologous Holliday Junctions (dagger). Biochemistry 2008
InteractionPhysicalInteraction Rv2593cactiveshahanup862012-10-05
Structural Analysis
JR. Prabu, S. Thamotharan et al. Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA Additional role of RuvB-binding domain and inter species variability. Biochim. Biophys. Acta 2009
InteractionPhysicalInteraction Rv2593cactiveshahanup862012-10-05
Structural Analysis
PC. Brooks, F. Movahedzadeh et al. Identification of some DNA damage-inducible genes of Mycobacterium tuberculosis: apparent lack of correlation with LexA binding. J. Bacteriol. 2001
InteractionPhysicalInteraction Rv2593cactiveshahanup862012-10-05
Structural Analysis
JR. Prabu, S. Thamotharan et al. Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2006
InteractionPhysicalInteraction Rv2593cactiveshahanup862012-10-05
Structural Analysis
authors,CV. Privezentzev,A. Keeley,B. Sigala,IR. Tsaneva The role of RuvA octamerization for RuvAB function in vitro and in vivo. J. Biol. Chem. 2005
InteractionPhysicalInteraction Rv2593cactiveshahanup862012-10-05
Structural Analysis
JS. Khanduja, P. Tripathi et al. Mycobacterium tuberculosis RuvA Induces Two Distinct Types of Structural Distortions between the Homologous and Heterologous Holliday Junctions (dagger). Biochemistry 2008
InteractionPhysicalInteraction Rv2593cactiveshahanup862012-10-05
Structural Analysis
JR. Prabu, S. Thamotharan et al. Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA Additional role of RuvB-binding domain and inter species variability. Biochim. Biophys. Acta 2009
InteractionPhysicalInteraction Rv2593cactiveshahanup862012-10-05
Structural Analysis
JR. Prabu, S. Thamotharan et al. Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2006
OtherTBPWY:Recombination repairactivevmizrahi2012-03-05
DNA Replication Fork Reversal Catalyzed by RuvAB Proteins functionally characterized