메뉴 건너뛰기




Volumn 1, Issue 2, 2012, Pages 194-213

Extracytoplasmic function σ factors of the widely distributed group ECF41 contain a fused regulatory domain

Author keywords

Anti factor; ECF factor; Signal transduction

Indexed keywords

CARBOXYLYASE; CARBOXYMUCONOLACTONE DECARBOXYLASE; EPIMERASE; EXTRACYTOPLASMIC FUNCTION PROTEIN 41; OXIDOREDUCTASE; SIGMA FACTOR; UNCLASSIFIED DRUG;

EID: 84873523437     PISSN: None     EISSN: 20458827     Source Type: Journal    
DOI: 10.1002/mbo3.22     Document Type: Article
Times cited : (34)

References (63)
  • 5
    • 8744309111 scopus 로고    scopus 로고
    • New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria
    • Arnaud, M., A. Chastanet, and M. Debarbouille. 2004. New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria. Appl. Environ. Microbiol. 70:6887-6891.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 6887-6891
    • Arnaud, M.1    Chastanet, A.2    Debarbouille, M.3
  • 6
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey, T. L., and C. Elkan. 1994. Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc. Int. Conf. Intell Syst. Mol. Biol. 2:28-36.
    • (1994) Proc. Int. Conf. Intell Syst. Mol. Biol. , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 8
    • 0035163555 scopus 로고    scopus 로고
    • Development and characterization of a xylose-dependent system for expression of cloned genes in Bacillus subtilis: conditional complementation of a teichoic acid mutant
    • Bhavsar, A. P., X. Zhao, and E. D. Brown. 2001. Development and characterization of a xylose-dependent system for expression of cloned genes in Bacillus subtilis: conditional complementation of a teichoic acid mutant. Appl. Environ. Microbiol. 67:403-410.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 403-410
    • Bhavsar, A.P.1    Zhao, X.2    Brown, E.D.3
  • 9
    • 0037379691 scopus 로고    scopus 로고
    • New technologies to assess genotype-phenotype relationships
    • Bochner, B. R. 2003. New technologies to assess genotype-phenotype relationships. Nat. Rev. Genet. 4:309-314.
    • (2003) Nat. Rev. Genet. , vol.4 , pp. 309-314
    • Bochner, B.R.1
  • 10
    • 84884212934 scopus 로고    scopus 로고
    • Low level analysis of high-density oligonucleotide array data: background, normalization and summarization. Dissertation at University of California, Berkeley, CA.
    • Bolstad, B. 2004. Low level analysis of high-density oligonucleotide array data: background, normalization and summarization. Dissertation at University of California, Berkeley, CA.
    • (2004)
    • Bolstad, B.1
  • 11
    • 0035075383 scopus 로고    scopus 로고
    • How sigma docks to RNA polymerase and what sigma does
    • Burgess, R. R., and L. Anthony. 2001. How sigma docks to RNA polymerase and what sigma does. Curr. Opin. Microbiol. 4:126-131.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 126-131
    • Burgess, R.R.1    Anthony, L.2
  • 12
    • 37349021513 scopus 로고    scopus 로고
    • Environmental sensing and the role of extracytoplasmic function (ECF) sigma factors
    • W.M. El-Sharoud, ed. Springer GmbH, Berlin, Heidelberg.
    • Butcher, B. G., T. Mascher, and J. D. Helmann. 2008. Environmental sensing and the role of extracytoplasmic function (ECF) sigma factors. Pp. 233-261 in W.M. El-Sharoud, ed. Bacterial physiology-a molecular approach. Springer GmbH, Berlin, Heidelberg.
    • (2008) Bacterial physiology-a molecular approach , pp. 233-261
    • Butcher, B.G.1    Mascher, T.2    Helmann, J.D.3
  • 14
    • 42049122814 scopus 로고    scopus 로고
    • Regulation of bacterial RNA polymerase sigma factor activity: a structural perspective
    • Campbell, E. A., L. F. Westblade, and S. A. Darst. 2008. Regulation of bacterial RNA polymerase sigma factor activity: a structural perspective. Curr. Opin. Microbiol. 11:121-127.
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 121-127
    • Campbell, E.A.1    Westblade, L.F.2    Darst, S.A.3
  • 16
    • 0027132539 scopus 로고
    • Amino-terminal amino acids modulate sigma-factor DNA-binding activity
    • Dombroski, A. J., W. A. Walter, and C. A. Gross. 1993. Amino-terminal amino acids modulate sigma-factor DNA-binding activity. Genes Dev. 7:2446-2455.
    • (1993) Genes Dev. , vol.7 , pp. 2446-2455
    • Dombroski, A.J.1    Walter, W.A.2    Gross, C.A.3
  • 17
    • 52949112607 scopus 로고    scopus 로고
    • Organization and evolution of the biological response to singlet oxygen stress
    • Dufour, Y. S., R. Landick, and T. J. Donohue. 2008. Organization and evolution of the biological response to singlet oxygen stress. J. Mol. Biol. 383:713-730.
    • (2008) J. Mol. Biol. , vol.383 , pp. 713-730
    • Dufour, Y.S.1    Landick, R.2    Donohue, T.J.3
  • 18
    • 77957325735 scopus 로고    scopus 로고
    • Reconstruction of the core and extended regulons of global transcription factors
    • Dufour, Y. S., P. J. Kiley, and T. J. Donohue. 2010. Reconstruction of the core and extended regulons of global transcription factors. PLoS Genet. 6:e1001027.
    • (2010) PLoS Genet. , vol.6
    • Dufour, Y.S.1    Kiley, P.J.2    Donohue, T.J.3
  • 19
    • 0742287185 scopus 로고    scopus 로고
    • Cupins: the most functionally diverse protein superfamily?
    • Dunwell, J. M., A. Purvis, and S. Khuri. 2004. Cupins: the most functionally diverse protein superfamily? Phytochemistry 65:7-17.
    • (2004) Phytochemistry , vol.65 , pp. 7-17
    • Dunwell, J.M.1    Purvis, A.2    Khuri, S.3
  • 20
    • 0031909725 scopus 로고    scopus 로고
    • Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity
    • Eulberg, D., S. Lakner, L. A. Golovleva, and M. Schlomann. 1998. Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity. J. Bacteriol. 180:1072-1081.
    • (1998) J. Bacteriol. , vol.180 , pp. 1072-1081
    • Eulberg, D.1    Lakner, S.2    Golovleva, L.A.3    Schlomann, M.4
  • 21
    • 0000122573 scopus 로고
    • PHYLIP-phylogeny inference package (version 3.2)
    • Felsenstein, J. 1989. PHYLIP-phylogeny inference package (version 3.2). Cladistics 5:164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 22
    • 55549086417 scopus 로고    scopus 로고
    • Streptomyces morphogenetics: dissecting differentiation in a filamentous bacterium
    • Flärdh, K., and M. J. Buttner. 2009. Streptomyces morphogenetics: dissecting differentiation in a filamentous bacterium. Nat. Rev. Microbiol. 7:36-49.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 36-49
    • Flärdh, K.1    Buttner, M.J.2
  • 24
    • 0242692671 scopus 로고    scopus 로고
    • Multiple sigma subunits and the partitioning of bacterial transcription space
    • Gruber, T. M., and C. A. Gross. 2003. Multiple sigma subunits and the partitioning of bacterial transcription space. Annu. Rev. Microbiol. 57:441-466.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 441-466
    • Gruber, T.M.1    Gross, C.A.2
  • 25
    • 0030597337 scopus 로고    scopus 로고
    • Plasmids for ectopic integration in Bacillus subtilis
    • Guerout-Fleury, A. M., N. Frandsen, and P. Stragier. 1996. Plasmids for ectopic integration in Bacillus subtilis. Gene 180:57-61.
    • (1996) Gene , vol.180 , pp. 57-61
    • Guerout-Fleury, A.M.1    Frandsen, N.2    Stragier, P.3
  • 26
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall, T. A. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl. Acids Symp. Ser. 41:95-98.
    • (1999) Nucl. Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 27
    • 71749105254 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis in the control of extracytoplasmic function sigma factors
    • Heinrich, J., and T. Wiegert. 2009. Regulated intramembrane proteolysis in the control of extracytoplasmic function sigma factors. Res. Microbiol. 160:696-703.
    • (2009) Res. Microbiol. , vol.160 , pp. 696-703
    • Heinrich, J.1    Wiegert, T.2
  • 28
    • 0035985580 scopus 로고    scopus 로고
    • The extracytoplasmic function (ECF) sigma factors
    • Helmann, J. D. 2002. The extracytoplasmic function (ECF) sigma factors. Adv. Microb. Physiol. 46:47-110.
    • (2002) Adv. Microb. Physiol. , vol.46 , pp. 47-110
    • Helmann, J.D.1
  • 29
    • 80052804067 scopus 로고    scopus 로고
    • Regulation by alternative sigma factors
    • G. Storz and R. Hengge, eds. ASM Press, Washington, DC.
    • Helmann, J. D. 2010. Regulation by alternative sigma factors. Pp. 31-43 in G. Storz and R. Hengge, eds. Bacterial stress responses. ASM Press, Washington, DC.
    • (2010) Bacterial stress responses , pp. 31-43
    • Helmann, J.D.1
  • 30
    • 0023918675 scopus 로고
    • Structure and function of bacterial sigma factors
    • Helmann, J. D., and M. J. Chamberlin. 1988. Structure and function of bacterial sigma factors. Annu. Rev. Biochem. 57:839-872.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 839-872
    • Helmann, J.D.1    Chamberlin, M.J.2
  • 32
    • 0036015637 scopus 로고    scopus 로고
    • A signal transduction system in Streptomyces coelicolor that activates the expression of a putative cell wall glycan operon in response to vancomycin and other cell wall-specific antibiotics
    • Hong, H. J., M. S. Paget, and M. J. Buttner. 2002. A signal transduction system in Streptomyces coelicolor that activates the expression of a putative cell wall glycan operon in response to vancomycin and other cell wall-specific antibiotics. Mol. Microbiol. 44:1199-1211.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1199-1211
    • Hong, H.J.1    Paget, M.S.2    Buttner, M.J.3
  • 33
    • 4143149555 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis sigJ gene controls sensitivity of the bacterium to hydrogen peroxide
    • Hu, Y., S. Kendall, N. G. Stoker, and A. R. Coates. 2004. The Mycobacterium tuberculosis sigJ gene controls sensitivity of the bacterium to hydrogen peroxide. FEMS Microbiol. Lett. 237:415-423.
    • (2004) FEMS Microbiol. Lett. , vol.237 , pp. 415-423
    • Hu, Y.1    Kendall, S.2    Stoker, N.G.3    Coates, A.R.4
  • 35
    • 33646147373 scopus 로고    scopus 로고
    • Crystal structure of the conserved protein TTHA0727 from Thermus thermophilus HB8 at 1.9 A resolution: a CMD family member distinct from carboxymuconolactone decarboxylase (CMD) and AhpD
    • Ito, K., R. Arai, E. Fusatomi, T. Kamo-Uchikubo, S. Kawaguchi, R. Akasaka, T. Terada, S. Kuramitsu, M. Shirouzu, and S. Yokoyama. 2006. Crystal structure of the conserved protein TTHA0727 from Thermus thermophilus HB8 at 1.9 A resolution: a CMD family member distinct from carboxymuconolactone decarboxylase (CMD) and AhpD. Protein Sci. 15:1187-1192.
    • (2006) Protein Sci. , vol.15 , pp. 1187-1192
    • Ito, K.1    Arai, R.2    Fusatomi, E.3    Kamo-Uchikubo, T.4    Kawaguchi, S.5    Akasaka, R.6    Terada, T.7    Kuramitsu, S.8    Shirouzu, M.9    Yokoyama, S.10
  • 36
    • 0030667399 scopus 로고    scopus 로고
    • K in controlling activity in transcription initiation
    • K in controlling activity in transcription initiation. J. Biol. Chem. 272:31029-31035.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31029-31035
    • Johnson, B.D.1    Dombroski, A.J.2
  • 38
    • 0043032814 scopus 로고    scopus 로고
    • The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics
    • Koshkin, A., C. M. Nunn, S. Djordjevic, and P. R. Ortiz de Montellano. 2003. The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics. J. Biol. Chem. 278:29502-29508.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29502-29508
    • Koshkin, A.1    Nunn, C.M.2    Djordjevic, S.3    Ortiz de Montellano, P.R.4
  • 40
    • 35048877274 scopus 로고    scopus 로고
    • The archaeon Methanosarcina acetivorans contains a protein disulfide reductase with an iron-sulfur cluster
    • Lessner, D. J., and J. G. Ferry. 2007. The archaeon Methanosarcina acetivorans contains a protein disulfide reductase with an iron-sulfur cluster. J. Bacteriol. 189:7475-7484.
    • (2007) J. Bacteriol. , vol.189 , pp. 7475-7484
    • Lessner, D.J.1    Ferry, J.G.2
  • 42
    • 0028018104 scopus 로고
    • Analysis of the Streptomyces coelicolor sigE gene reveals the existence of a subfamily of eubacterial RNA polymerase sigma factors involved in the regulation of extracytoplasmic functions
    • Lonetto, M. A., K. L. Brown, K. E. Rudd, and M. J. Buttner. 1994. Analysis of the Streptomyces coelicolor sigE gene reveals the existence of a subfamily of eubacterial RNA polymerase sigma factors involved in the regulation of extracytoplasmic functions. Proc. Natl. Acad. Sci. USA 91:7573-7577.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7573-7577
    • Lonetto, M.A.1    Brown, K.L.2    Rudd, K.E.3    Buttner, M.J.4
  • 44
    • 0025637607 scopus 로고
    • K, may depend on events occurring in the forespore during Bacillus subtilis development
    • K, may depend on events occurring in the forespore during Bacillus subtilis development. Proc. Natl. Acad. Sci. USA 87:9722-9726.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9722-9726
    • Lu, S.1    Halberg, R.2    Kroos, L.3
  • 45
    • 47749087475 scopus 로고    scopus 로고
    • A previously unidentified sigma factor and two accessory proteins regulate oxalate decarboxylase expression in Bacillus subtilis
    • MacLellan, S. R., T. Wecke, and J. D. Helmann. 2008. A previously unidentified sigma factor and two accessory proteins regulate oxalate decarboxylase expression in Bacillus subtilis. Mol. Microbiol. 69:954-967.
    • (2008) Mol. Microbiol. , vol.69 , pp. 954-967
    • MacLellan, S.R.1    Wecke, T.2    Helmann, J.D.3
  • 46
  • 48
    • 27944453600 scopus 로고    scopus 로고
    • Virtual Footprint and PRODORIC: an integrative framework for regulon prediction in prokaryotes
    • Münch, R., K. Hiller, A. Grote, M. Scheer, J. Klein, M. Schobert, and D. Jahn. 2005. Virtual Footprint and PRODORIC: an integrative framework for regulon prediction in prokaryotes. Bioinformatics 21:4187-4189.
    • (2005) Bioinformatics , vol.21 , pp. 4187-4189
    • Münch, R.1    Hiller, K.2    Grote, A.3    Scheer, M.4    Klein, J.5    Schobert, M.6    Jahn, D.7
  • 49
    • 27144523463 scopus 로고    scopus 로고
    • Construction of plasmid-based expression vectors for Bacillus subtilis exhibiting full structural stability
    • Nguyen, H. D., Q. A. Nguyen, R. C. Ferreira, L. C. S. Ferreira, L. T. Tran, and W. Schumann. 2005. Construction of plasmid-based expression vectors for Bacillus subtilis exhibiting full structural stability. Plasmid 54:241-248.
    • (2005) Plasmid , vol.54 , pp. 241-248
    • Nguyen, H.D.1    Nguyen, Q.A.2    Ferreira, R.C.3    Ferreira, L.C.S.4    Tran, L.T.5    Schumann, W.6
  • 52
    • 0021592032 scopus 로고
    • In vitro insertional mutagenesis with a selectable DNA fragment
    • Prentki, P., and H. M. Krisch. 1984. In vitro insertional mutagenesis with a selectable DNA fragment. Gene 29:303-313.
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 54
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz, J., F. Milpetz, P. Bork, and C. P. Ponting. 1998. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. USA 95:5857-5864.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 55
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Biotechnology 1:784-791.
    • (1983) Biotechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 56
    • 72849182812 scopus 로고
    • A requirement for sodium in the growth of Rhodopseudomonas spheroides
    • Sistrom, W. R. 1960. A requirement for sodium in the growth of Rhodopseudomonas spheroides. J. Gen. Microbiol. 22:778-785.
    • (1960) J. Gen. Microbiol. , vol.22 , pp. 778-785
    • Sistrom, W.R.1
  • 58
    • 0035803486 scopus 로고    scopus 로고
    • The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases
    • Stammers, D. K., J. Ren, K. Leslie, C. E. Nichols, H. K. Lamb, S. Cocklin, A. Dodds, and A. R. Hawkins. 2001. The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases. Embo. J. 20:6619-6626.
    • (2001) Embo. J. , vol.20 , pp. 6619-6626
    • Stammers, D.K.1    Ren, J.2    Leslie, K.3    Nichols, C.E.4    Lamb, H.K.5    Cocklin, S.6    Dodds, A.7    Hawkins, A.R.8
  • 59
    • 70350432754 scopus 로고    scopus 로고
    • The third pillar of bacterial signal transduction: classification of the extracytoplasmic function (ECF) σ factor protein family
    • Staroń, A., H. J. Sofia, S. Dietrich, L. E. Ulrich, H. Liesegang, and T. Mascher. 2009. The third pillar of bacterial signal transduction: classification of the extracytoplasmic function (ECF) σ factor protein family. Mol. Microbiol. 74:557-581.
    • (2009) Mol. Microbiol. , vol.74 , pp. 557-581
    • Staroń, A.1    Sofia, H.J.2    Dietrich, S.3    Ulrich, L.E.4    Liesegang, H.5    Mascher, T.6
  • 60
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 61
    • 75549092201 scopus 로고    scopus 로고
    • The MiST2 database: a comprehensive genomics resource on microbial signal transduction
    • Ulrich, L. E., and I. B. Zhulin. 2010. The MiST2 database: a comprehensive genomics resource on microbial signal transduction. Nucleic Acids Res. 38:D401-D407.
    • (2010) Nucleic Acids Res. , vol.38
    • Ulrich, L.E.1    Zhulin, I.B.2
  • 63
    • 0031596513 scopus 로고    scopus 로고
    • K promotes membrane association and inhibits RNA polymerase core binding
    • K promotes membrane association and inhibits RNA polymerase core binding. J. Bacteriol. 180:2434-2441.
    • (1998) J. Bacteriol. , vol.180 , pp. 2434-2441
    • Zhang, B.1    Hofmeister, A.2    Kroos, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.