Difference between revisions of "Spo0A"
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|style="background:#ABCDEF;" align="center"|'''Function''' || initiation of sporulation | |style="background:#ABCDEF;" align="center"|'''Function''' || initiation of sporulation | ||
|- | |- | ||
− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/biofilm.html Biofilm], [http://subtiwiki.uni-goettingen.de/pathways/gene_regulation_nucleotides.html Nucleotides (regulation)], [http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate], [http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism],<br/>[http://subtiwiki.uni-goettingen.de/pathways/carbohydrate_metabolic_pathways.html Sugar catabolism], [http://subtiwiki.uni-goettingen.de/pathways/stress_response.html Stress], [http://subtiwiki.uni-goettingen.de/pathways/tRNA_charging.html tRNA charging]''' | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/biofilm.html Biofilm], [http://subtiwiki.uni-goettingen.de/pathways/biofilm.html Biofilm], [http://subtiwiki.uni-goettingen.de/pathways/gene_regulation_nucleotides.html Nucleotides (regulation)], [http://subtiwiki.uni-goettingen.de/pathways/glutamate.html Ammonium/ glutamate], [http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism],<br/>[http://subtiwiki.uni-goettingen.de/pathways/carbohydrate_metabolic_pathways.html Sugar catabolism], [http://subtiwiki.uni-goettingen.de/pathways/stress_response.html Stress], [http://subtiwiki.uni-goettingen.de/pathways/tRNA_charging.html tRNA charging]''' |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 29 kDa, 5.989 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 29 kDa, 5.989 |
Revision as of 13:59, 16 February 2010
- Description: phosphorelay regulator, initiation of sporulation
Gene name | spo0A |
Synonyms | spo0C, spo0G, spoIIL, sof-1 |
Essential | no |
Product | phosphorelay response regulator |
Function | initiation of sporulation |
Metabolic function and regulation of this protein in SubtiPathways: Biofilm, Biofilm, Nucleotides (regulation), Ammonium/ glutamate, Central C-metabolism, Sugar catabolism, Stress, tRNA charging | |
MW, pI | 29 kDa, 5.989 |
Gene length, protein length | 801 bp, 267 aa |
Immediate neighbours | yqiG, spoIVB |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU24220
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Genes controlled by Spo0A
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: receives phosphorylation from Spo0B, dephosphorylation by Spo0E, direct phosphorylation by KinC upon potassium leakage PubMed
- Cofactor(s):
- Effectors of protein activity: the phosphorylation state affects DNA binding activity
- Localization:
Database entries
- Structure: 1QMP (with phosphorylated aspartate, Geobacillus stearothermophilus), 1FC3 (trans-activation domain, Geobacillus stearothermophilus), 1LQ1 (complex with DNA)
- UniProt: P06534
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: spo0A PubMed
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Tony Wilkinson, York University, U.K. homepage
- Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage
- Charles Moran, Emory University, NC, USA homepage
Your additional remarks
References
Reviews
Original Publications
Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Heterochronic phosphorelay gene expression as a source of heterogeneity in Bacillus subtilis spore formation.
J Bacteriol: 2010, 192(8);2053-67
[PubMed:20154131]
[WorldCat.org]
[DOI]
(I p)
Steve D Seredick, Barbara M Seredick, David Baker, George B Spiegelman
An A257V mutation in the bacillus subtilis response regulator Spo0A prevents regulated expression of promoters with low-consensus binding sites.
J Bacteriol: 2009, 191(17);5489-98
[PubMed:19581368]
[WorldCat.org]
[DOI]
(I p)
Virginia Castilla-Llorente, Wilfried J J Meijer, Margarita Salas
Differential Spo0A-mediated effects on transcription and replication of the related Bacillus subtilis phages Nf and phi29 explain their different behaviours in vivo.
Nucleic Acids Res: 2009, 37(15);4955-64
[PubMed:19528067]
[WorldCat.org]
[DOI]
(I p)
Virginia Castilla-Llorente, Margarita Salas, Wilfried J J Meijer
Different responses to Spo0A-mediated suppression of the related Bacillus subtilis phages Nf and phi29.
Environ Microbiol: 2009, 11(5);1137-49
[PubMed:19207565]
[WorldCat.org]
[DOI]
(I p)
Daniel López, Michael A Fischbach, Frances Chu, Richard Losick, Roberto Kolter
Structurally diverse natural products that cause potassium leakage trigger multicellularity in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2009, 106(1);280-5
[PubMed:19114652]
[WorldCat.org]
[DOI]
(I p)
Daniel T Verhamme, Ewan J Murray, Nicola R Stanley-Wall
DegU and Spo0A jointly control transcription of two loci required for complex colony development by Bacillus subtilis.
J Bacteriol: 2009, 191(1);100-8
[PubMed:18978066]
[WorldCat.org]
[DOI]
(I p)
Allison V Banse, Arnaud Chastanet, Lilah Rahn-Lee, Errett C Hobbs, Richard Losick
Parallel pathways of repression and antirepression governing the transition to stationary phase in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2008, 105(40);15547-52
[PubMed:18840696]
[WorldCat.org]
[DOI]
(I p)
Amrita Kumar, Charles P Moran
Promoter activation by repositioning of RNA polymerase.
J Bacteriol: 2008, 190(9);3110-7
[PubMed:18296515]
[WorldCat.org]
[DOI]
(I p)
Guangnan Chen, Amrita Kumar, Travis H Wyman, Charles P Moran
Spo0A-dependent activation of an extended -10 region promoter in Bacillus subtilis.
J Bacteriol: 2006, 188(4);1411-8
[PubMed:16452424]
[WorldCat.org]
[DOI]
(P p)
Jessica M Silvaggi, John B Perkins, Richard Losick
Genes for small, noncoding RNAs under sporulation control in Bacillus subtilis.
J Bacteriol: 2006, 188(2);532-41
[PubMed:16385044]
[WorldCat.org]
[DOI]
(P p)
Masaya Fujita, Richard Losick
Evidence that entry into sporulation in Bacillus subtilis is governed by a gradual increase in the level and activity of the master regulator Spo0A.
Genes Dev: 2005, 19(18);2236-44
[PubMed:16166384]
[WorldCat.org]
[DOI]
(P p)
Masaya Fujita, José Eduardo González-Pastor, Richard Losick
High- and low-threshold genes in the Spo0A regulon of Bacillus subtilis.
J Bacteriol: 2005, 187(4);1357-68
[PubMed:15687200]
[WorldCat.org]
[DOI]
(P p)
Steve D Seredick, George B Spiegelman
The Bacillus subtilis response regulator Spo0A stimulates sigmaA-dependent transcription prior to the major energetic barrier.
J Biol Chem: 2004, 279(17);17397-403
[PubMed:14976210]
[WorldCat.org]
[DOI]
(P p)
Amrita Kumar, James A Brannigan, Charles P Moran
Alpha-helix E of Spo0A is required for sigmaA- but not for sigmaH-dependent promoter activation in Bacillus subtilis.
J Bacteriol: 2004, 186(4);1078-83
[PubMed:14762002]
[WorldCat.org]
[DOI]
(P p)
Amrita Kumar, Cindy Buckner Starke, Mark DeZalia, Charles P Moran
Surfaces of Spo0A and RNA polymerase sigma factor A that interact at the spoIIG promoter in Bacillus subtilis.
J Bacteriol: 2004, 186(1);200-6
[PubMed:14679239]
[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)
Masaya Fujita, Richard Losick
The master regulator for entry into sporulation in Bacillus subtilis becomes a cell-specific transcription factor after asymmetric division.
Genes Dev: 2003, 17(9);1166-74
[PubMed:12730135]
[WorldCat.org]
[DOI]
(P p)
Shigeo Hosoya, Kei Asai, Naotake Ogasawara, Michio Takeuchi, Tsutomu Sato
Mutation in yaaT leads to significant inhibition of phosphorelay during sporulation in Bacillus subtilis.
J Bacteriol: 2002, 184(20);5545-53
[PubMed:12270811]
[WorldCat.org]
[DOI]
(P p)
Haiyan Zhao, Tarek Msadek, James Zapf, Madhusudan, James A Hoch, Kottayil I Varughese
DNA complexed structure of the key transcription factor initiating development in sporulating bacteria.
Structure: 2002, 10(8);1041-50
[PubMed:12176382]
[WorldCat.org]
[DOI]
(P p)
Sophie J Stephenson, Marta Perego
Interaction surface of the Spo0A response regulator with the Spo0E phosphatase.
Mol Microbiol: 2002, 44(6);1455-67
[PubMed:12067336]
[WorldCat.org]
[DOI]
(P p)
M Perego
A new family of aspartyl phosphate phosphatases targeting the sporulation transcription factor Spo0A of Bacillus subtilis.
Mol Microbiol: 2001, 42(1);133-43
[PubMed:11679073]
[WorldCat.org]
[DOI]
(P p)
C Eymann, G Mittenhuber, M Hecker
The stringent response, sigmaH-dependent gene expression and sporulation in Bacillus subtilis.
Mol Gen Genet: 2001, 264(6);913-23
[PubMed:11254139]
[WorldCat.org]
[DOI]
(P p)
H Nanamiya, K Takahashi, M Fujita, F Kawamura
Deficiency of the initiation events of sporulation in Bacillus subtilis clpP mutant can be suppressed by a lack of the Spo0E protein phosphatase.
Biochem Biophys Res Commun: 2000, 279(1);229-33
[PubMed:11112444]
[WorldCat.org]
[DOI]
(P p)
M Jiang, W Shao, M Perego, J A Hoch
Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis.
Mol Microbiol: 2000, 38(3);535-42
[PubMed:11069677]
[WorldCat.org]
[DOI]
(P p)
P Fawcett, P Eichenberger, R Losick, P Youngman
The transcriptional profile of early to middle sporulation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2000, 97(14);8063-8
[PubMed:10869437]
[WorldCat.org]
[DOI]
(P p)
C M Buckner, C P Moran
A region in Bacillus subtilis sigmaH required for Spo0A-dependent promoter activity.
J Bacteriol: 1998, 180(18);4987-90
[PubMed:9733708]
[WorldCat.org]
[DOI]
(P p)
C M Buckner, G Schyns, C P Moran
A region in the Bacillus subtilis transcription factor Spo0A that is important for spoIIG promoter activation.
J Bacteriol: 1998, 180(14);3578-83
[PubMed:9658000]
[WorldCat.org]
[DOI]
(P p)
A Khvorova, L Zhang, M L Higgins, P J Piggot
The spoIIE locus is involved in the Spo0A-dependent switch in the location of FtsZ rings in Bacillus subtilis.
J Bacteriol: 1998, 180(5);1256-60
[PubMed:9495766]
[WorldCat.org]
[DOI]
(P p)
C E Grimshaw, S Huang, C G Hanstein, M A Strauch, D Burbulys, L Wang, J A Hoch, J M Whiteley
Synergistic kinetic interactions between components of the phosphorelay controlling sporulation in Bacillus subtilis.
Biochemistry: 1998, 37(5);1365-75
[PubMed:9477965]
[WorldCat.org]
[DOI]
(P p)
G Schyns, C M Buckner, C P Moran
Activation of the Bacillus subtilis spoIIG promoter requires interaction of Spo0A and the sigma subunit of RNA polymerase.
J Bacteriol: 1997, 179(17);5605-8
[PubMed:9287022]
[WorldCat.org]
[DOI]
(P p)
L V Wray, A E Ferson, S H Fisher
Expression of the Bacillus subtilis ureABC operon is controlled by multiple regulatory factors including CodY, GlnR, TnrA, and Spo0H.
J Bacteriol: 1997, 179(17);5494-501
[PubMed:9287005]
[WorldCat.org]
[DOI]
(P p)
M Perego, P Glaser, J A Hoch
Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis.
Mol Microbiol: 1996, 19(6);1151-7
[PubMed:8730857]
[WorldCat.org]
[DOI]
(P p)
P A Levin, R Losick
Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis.
Genes Dev: 1996, 10(4);478-88
[PubMed:8600030]
[WorldCat.org]
[DOI]
(P p)
J Hahn, M Roggiani, D Dubnau
The major role of Spo0A in genetic competence is to downregulate abrB, an essential competence gene.
J Bacteriol: 1995, 177(12);3601-5
[PubMed:7768874]
[WorldCat.org]
[DOI]
(P p)
J K Grimsley, R B Tjalkens, M A Strauch, T H Bird, G B Spiegelman, Z Hostomsky, J M Whiteley, J A Hoch
Subunit composition and domain structure of the Spo0A sporulation transcription factor of Bacillus subtilis.
J Biol Chem: 1994, 269(24);16977-82
[PubMed:8207022]
[WorldCat.org]
(P p)
K L Ohlsen, J K Grimsley, J A Hoch
Deactivation of the sporulation transcription factor Spo0A by the Spo0E protein phosphatase.
Proc Natl Acad Sci U S A: 1994, 91(5);1756-60
[PubMed:8127878]
[WorldCat.org]
[DOI]
(P p)
J M Baldus, B D Green, P Youngman, C P Moran
Phosphorylation of Bacillus subtilis transcription factor Spo0A stimulates transcription from the spoIIG promoter by enhancing binding to weak 0A boxes.
J Bacteriol: 1994, 176(2);296-306
[PubMed:8288522]
[WorldCat.org]
[DOI]
(P p)
T H Bird, J K Grimsley, J A Hoch, G B Spiegelman
Phosphorylation of Spo0A activates its stimulation of in vitro transcription from the Bacillus subtilis spoIIG operon.
Mol Microbiol: 1993, 9(4);741-9
[PubMed:8231806]
[WorldCat.org]
[DOI]
(P p)
K K Jensen, E Sharkova, M F Duggan, Y Qi, A Koide, J A Hoch, F M Hulett
Bacillus subtilis transcription regulator, Spo0A, decreases alkaline phosphatase levels induced by phosphate starvation.
J Bacteriol: 1993, 175(12);3749-56
[PubMed:8509330]
[WorldCat.org]
[DOI]
(P p)
M A Strauch, K A Trach, J Day, J A Hoch
Spo0A activates and represses its own synthesis by binding at its dual promoters.
Biochimie: 1992, 74(7-8);619-26
[PubMed:1391039]
[WorldCat.org]
[DOI]
(P p)
M Predich, G Nair, I Smith
Bacillus subtilis early sporulation genes kinA, spo0F, and spo0A are transcribed by the RNA polymerase containing sigma H.
J Bacteriol: 1992, 174(9);2771-8
[PubMed:1569009]
[WorldCat.org]
[DOI]
(P p)
K York, T J Kenney, S Satola, C P Moran, H Poth, P Youngman
Spo0A controls the sigma A-dependent activation of Bacillus subtilis sporulation-specific transcription unit spoIIE.
J Bacteriol: 1992, 174(8);2648-58
[PubMed:1556084]
[WorldCat.org]
[DOI]
(P p)
S W Satola, J M Baldus, C P Moran
Binding of Spo0A stimulates spoIIG promoter activity in Bacillus subtilis.
J Bacteriol: 1992, 174(5);1448-53
[PubMed:1537790]
[WorldCat.org]
[DOI]
(P p)
M Perego, J J Wu, G B Spiegelman, J A Hoch
Mutational dissociation of the positive and negative regulatory properties of the Spo0A sporulation transcription factor of Bacillus subtilis.
Gene: 1991, 100;207-12
[PubMed:1905258]
[WorldCat.org]
[DOI]
(P p)
D Burbulys, K A Trach, J A Hoch
Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay.
Cell: 1991, 64(3);545-52
[PubMed:1846779]
[WorldCat.org]
[DOI]
(P p)
U Bai, M Lewandoski, E Dubnau, I Smith
Temporal regulation of the Bacillus subtilis early sporulation gene spo0F.
J Bacteriol: 1990, 172(9);5432-9
[PubMed:2118512]
[WorldCat.org]
[DOI]
(P p)
G Spiegelman, B Van Hoy, M Perego, J Day, K Trach, J A Hoch
Structural alterations in the Bacillus subtilis Spo0A regulatory protein which suppress mutations at several spo0 loci.
J Bacteriol: 1990, 172(9);5011-9
[PubMed:2118505]
[WorldCat.org]
[DOI]
(P p)
M Strauch, V Webb, G Spiegelman, J A Hoch
The SpoOA protein of Bacillus subtilis is a repressor of the abrB gene.
Proc Natl Acad Sci U S A: 1990, 87(5);1801-5
[PubMed:2106683]
[WorldCat.org]
[DOI]
(P p)
M Perego, G B Spiegelman, J A Hoch
Structure of the gene for the transition state regulator, abrB: regulator synthesis is controlled by the spo0A sporulation gene in Bacillus subtilis.
Mol Microbiol: 1988, 2(6);689-99
[PubMed:3145384]
[WorldCat.org]
[DOI]
(P p)
P Zuber, R Losick
Role of AbrB in Spo0A- and Spo0B-dependent utilization of a sporulation promoter in Bacillus subtilis.
J Bacteriol: 1987, 169(5);2223-30
[PubMed:2437099]
[WorldCat.org]
[DOI]
(P p)
F A Ferrari, K Trach, D LeCoq, J Spence, E Ferrari, J A Hoch
Characterization of the spo0A locus and its deduced product.
Proc Natl Acad Sci U S A: 1985, 82(9);2647-51
[PubMed:3157992]
[WorldCat.org]
[DOI]
(P p)
J A Hoch, K Trach, F Kawamura, H Saito
Identification of the transcriptional suppressor sof-1 as an alteration in the spo0A protein.
J Bacteriol: 1985, 161(2);552-5
[PubMed:2981817]
[WorldCat.org]
[DOI]
(P p)