메뉴 건너뛰기




Volumn 7, Issue 4, 2012, Pages

Mutational analysis of Cvab, an ABC transporter involved in the secretion of active colicin V

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ASPARTIC ACID; COLICIN; COLICIN V; CYSTEINE; GLUTAMINE; GLYCINE; HISTIDINE; LEUCINE; MUTANT PROTEIN; PROLINE; PROTEIN CVAB; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE; CVAB PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN;

EID: 84859994125     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035382     Document Type: Article
Times cited : (10)

References (34)
  • 1
    • 0028271859 scopus 로고
    • Purification and characterization of colicin V from Escherichia coli culture supernatants
    • Fath MJ, Zhang LH, Rush J, Kolter R, (1994) Purification and characterization of colicin V from Escherichia coli culture supernatants. Biochemistry 33: 6911-6917.
    • (1994) Biochemistry , vol.33 , pp. 6911-6917
    • Fath, M.J.1    Zhang, L.H.2    Rush, J.3    Kolter, R.4
  • 2
    • 0025134451 scopus 로고
    • Genetic analysis of an MDR-like export system: the secretion of colicin V
    • Gilson L, Mahanty HK, Kolter R, (1990) Genetic analysis of an MDR-like export system: the secretion of colicin V. EMBO J 9: 3875-3884.
    • (1990) EMBO J , vol.9 , pp. 3875-3884
    • Gilson, L.1    Mahanty, H.K.2    Kolter, R.3
  • 4
    • 0031894325 scopus 로고    scopus 로고
    • When an ATPase is not an ATPase: at low temperatures the C-terminal domain of the ABC transporter CvaB is a GTPase
    • Zhong X, Tai PC, (1998) When an ATPase is not an ATPase: at low temperatures the C-terminal domain of the ABC transporter CvaB is a GTPase. J Bacteriol 180: 1347-1353.
    • (1998) J Bacteriol , vol.180 , pp. 1347-1353
    • Zhong, X.1    Tai, P.C.2
  • 5
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst P, Elferink RO, (2002) Mammalian ABC transporters in health and disease. Annu Rev Biochem 71: 537-592.
    • (2002) Annu Rev Biochem , vol.71 , pp. 537-592
    • Borst, P.1    Elferink, R.O.2
  • 6
    • 0024329881 scopus 로고
    • The biochemistry of P-glycoprotein-mediated multidrug resistance
    • Endicott JA, Ling V, (1989) The biochemistry of P-glycoprotein-mediated multidrug resistance. Annu Rev Biochem 58: 137-171.
    • (1989) Annu Rev Biochem , vol.58 , pp. 137-171
    • Endicott, J.A.1    Ling, V.2
  • 7
    • 0037013262 scopus 로고    scopus 로고
    • The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover
    • Aleksandrov L, Aleksandrov AA, Chang XB, Riordan JR, (2002) The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover. J Biol Chem 277: 15419-15425.
    • (2002) J Biol Chem , vol.277 , pp. 15419-15425
    • Aleksandrov, L.1    Aleksandrov, A.A.2    Chang, X.B.3    Riordan, J.R.4
  • 8
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA
    • Riordan JR, Rommens JM, Kerem B, Alon N, Rozmahel R, et al. (1989) Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245: 1066-1073.
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1    Rommens, J.M.2    Kerem, B.3    Alon, N.4    Rozmahel, R.5
  • 9
    • 0029013783 scopus 로고
    • A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export
    • Havarstein LS, Diep DB, Nes IF, (1995) A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export. Mol Microbiol 16: 229-240.
    • (1995) Mol Microbiol , vol.16 , pp. 229-240
    • Havarstein, L.S.1    Diep, D.B.2    Nes, I.F.3
  • 10
    • 0345832155 scopus 로고    scopus 로고
    • Cys32 and His105 are the critical residues for the calcium-dependent cysteine proteolytic activity of CvaB, an ATP-binding cassette transporter
    • Wu KH, Tai PC, (2004) Cys32 and His105 are the critical residues for the calcium-dependent cysteine proteolytic activity of CvaB, an ATP-binding cassette transporter. J Biol Chem 279: 901-909.
    • (2004) J Biol Chem , vol.279 , pp. 901-909
    • Wu, K.H.1    Tai, P.C.2
  • 11
    • 0025949236 scopus 로고
    • Mutational analysis of the putative catalytic triad of the cowpea mosaic virus 24K protease
    • Dessens JT, Lomonossoff GP, (1991) Mutational analysis of the putative catalytic triad of the cowpea mosaic virus 24K protease. Virology 184: 738-746.
    • (1991) Virology , vol.184 , pp. 738-746
    • Dessens, J.T.1    Lomonossoff, G.P.2
  • 12
    • 0029930588 scopus 로고    scopus 로고
    • Contribution to activity of histidine-aromatic, amide-aromatic, and aromatic-aromatic interactions in the extended catalytic site of cysteine proteinases
    • Bromme D, Bonneau PR, Purisima E, Lachance P, Hajnik S, et al. (1996) Contribution to activity of histidine-aromatic, amide-aromatic, and aromatic-aromatic interactions in the extended catalytic site of cysteine proteinases. Biochemistry 35: 3970-3979.
    • (1996) Biochemistry , vol.35 , pp. 3970-3979
    • Bromme, D.1    Bonneau, P.R.2    Purisima, E.3    Lachance, P.4    Hajnik, S.5
  • 13
    • 0029072912 scopus 로고
    • Structural and functional roles of asparagine 175 in the cysteine protease papain
    • Vernet T, Tessier DC, Chatellier J, Plouffe C, Lee TS, et al. (1995) Structural and functional roles of asparagine 175 in the cysteine protease papain. J Biol Chem 270: 16645-16652.
    • (1995) J Biol Chem , vol.270 , pp. 16645-16652
    • Vernet, T.1    Tessier, D.C.2    Chatellier, J.3    Plouffe, C.4    Lee, T.S.5
  • 14
    • 0034696811 scopus 로고    scopus 로고
    • Evidence for tryptophan in proximity to histidine and cysteine as essential to the active site of an alkaline protease
    • Tanksale AM, Vernekar JV, Ghatge MS, Deshpande VV, (2000) Evidence for tryptophan in proximity to histidine and cysteine as essential to the active site of an alkaline protease. Biochem Biophys Res Commun 270: 910-917.
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 910-917
    • Tanksale, A.M.1    Vernekar, J.V.2    Ghatge, M.S.3    Deshpande, V.V.4
  • 15
    • 0026003243 scopus 로고
    • Contribution of the glutamine 19 side chain to transition-state stabilization in the oxyanion hole of papain
    • Menard R, Carriere J, Laflamme P, Plouffe C, Khouri HE, et al. (1991) Contribution of the glutamine 19 side chain to transition-state stabilization in the oxyanion hole of papain. Biochemistry 30: 8924-8928.
    • (1991) Biochemistry , vol.30 , pp. 8924-8928
    • Menard, R.1    Carriere, J.2    Laflamme, P.3    Plouffe, C.4    Khouri, H.E.5
  • 16
    • 0025376135 scopus 로고
    • A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain
    • Menard R, Khouri HE, Plouffe C, Dupras R, Ripoll D, et al. (1990) A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain. Biochemistry 29: 6706-6713.
    • (1990) Biochemistry , vol.29 , pp. 6706-6713
    • Menard, R.1    Khouri, H.E.2    Plouffe, C.3    Dupras, R.4    Ripoll, D.5
  • 17
    • 0017138215 scopus 로고
    • Binding of chloromethyl ketone substrate analogues to crystalline papain
    • Drenth J, Kalk KH, Swen HM, (1976) Binding of chloromethyl ketone substrate analogues to crystalline papain. Biochemistry 15: 3731-3738.
    • (1976) Biochemistry , vol.15 , pp. 3731-3738
    • Drenth, J.1    Kalk, K.H.2    Swen, H.M.3
  • 18
    • 0026885447 scopus 로고
    • Oxyanion hole interactions in serine and cysteine proteases
    • Menard R, Storer AC, (1992) Oxyanion hole interactions in serine and cysteine proteases. Biol Chem Hoppe Seyler 373: 393-400.
    • (1992) Biol Chem Hoppe Seyler , vol.373 , pp. 393-400
    • Menard, R.1    Storer, A.C.2
  • 19
    • 12944300453 scopus 로고    scopus 로고
    • The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium
    • Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, et al. (2000) The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proc Natl Acad Sci U S A 97: 588-592.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 588-592
    • Strobl, S.1    Fernandez-Catalan, C.2    Braun, M.3    Huber, R.4    Masumoto, H.5
  • 20
    • 33646179437 scopus 로고    scopus 로고
    • Expression and characterization of the peptidase domain of Streptococcus pneumoniae ComA, a bifunctional ATP-binding cassette transporter involved in quorum sensing pathway
    • Ishii S, Yano T, Hayashi H, (2006) Expression and characterization of the peptidase domain of Streptococcus pneumoniae ComA, a bifunctional ATP-binding cassette transporter involved in quorum sensing pathway. The Journal of biological chemistry 281: 4726-4731.
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 4726-4731
    • Ishii, S.1    Yano, T.2    Hayashi, H.3
  • 21
    • 33646179437 scopus 로고    scopus 로고
    • Expression and characterization of the peptidase domain of Streptococcus pneumoniae ComA, a bifunctional ATP-binding cassette transporter involved in quorum sensing pathway
    • Ishii S, Yano T, Hayashi H, (2006) Expression and characterization of the peptidase domain of Streptococcus pneumoniae ComA, a bifunctional ATP-binding cassette transporter involved in quorum sensing pathway. J Biol Chem 281: 4726-4731.
    • (2006) J Biol Chem , vol.281 , pp. 4726-4731
    • Ishii, S.1    Yano, T.2    Hayashi, H.3
  • 22
    • 2542450034 scopus 로고    scopus 로고
    • Molecular cloning, functional expression in Escherichia coli and enzymatic characterisation of a cysteine protease from white clover (Trifolium repens)
    • Asp T, Bowra S, Borg S, Holm PB, (2004) Molecular cloning, functional expression in Escherichia coli and enzymatic characterisation of a cysteine protease from white clover (Trifolium repens). Biochimica et biophysica acta 1699: 111-122.
    • (2004) Biochimica Et Biophysica Acta , vol.1699 , pp. 111-122
    • Asp, T.1    Bowra, S.2    Borg, S.3    Holm, P.B.4
  • 23
    • 11144230028 scopus 로고    scopus 로고
    • The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases
    • Im YJ, Na Y, Kang GB, Rho SH, Kim MK, et al. (2004) The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases. The Journal of biological chemistry 279: 53451-53457.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 53451-53457
    • Im, Y.J.1    Na, Y.2    Kang, G.B.3    Rho, S.H.4    Kim, M.K.5
  • 24
    • 16244367063 scopus 로고    scopus 로고
    • A novel cysteine protease HeLa DUB-1 responsible for cleaving the ubiquitin in human ovarian cancer cells
    • Kim MS, Yoo KJ, Kang I, Chung HM, Baek KH, (2004) A novel cysteine protease HeLa DUB-1 responsible for cleaving the ubiquitin in human ovarian cancer cells. International journal of oncology 25: 373-379.
    • (2004) International Journal of Oncology , vol.25 , pp. 373-379
    • Kim, M.S.1    Yoo, K.J.2    Kang, I.3    Chung, H.M.4    Baek, K.H.5
  • 25
    • 0031051894 scopus 로고    scopus 로고
    • Enzyme-substrate interaction in the catalytic triad of serine proteases: increase in the pKa of Asp102
    • Neuvonen H, (1997) Enzyme-substrate interaction in the catalytic triad of serine proteases: increase in the pKa of Asp102. Biochem J 322 (Pt 1): 351-352.
    • (1997) Biochem J , vol.322 , Issue.Pt 1 , pp. 351-352
    • Neuvonen, H.1
  • 26
    • 0023204278 scopus 로고
    • The catalytic role of the active site aspartic acid in serine proteases
    • Craik CS, Roczniak S, Largman C, Rutter WJ, (1987) The catalytic role of the active site aspartic acid in serine proteases. Science 237: 909-913.
    • (1987) Science , vol.237 , pp. 909-913
    • Craik, C.S.1    Roczniak, S.2    Largman, C.3    Rutter, W.J.4
  • 27
    • 0347719364 scopus 로고    scopus 로고
    • The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site
    • Zhu M, Shao F, Innes RW, Dixon JE, Xu Z, (2004) The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site. Proc Natl Acad Sci U S A 101: 302-307.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 302-307
    • Zhu, M.1    Shao, F.2    Innes, R.W.3    Dixon, J.E.4    Xu, Z.5
  • 28
    • 0026525805 scopus 로고
    • Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability
    • Loewenthal R, Sancho J, Fersht AR, (1992) Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. J Mol Biol 224: 759-770.
    • (1992) J Mol Biol , vol.224 , pp. 759-770
    • Loewenthal, R.1    Sancho, J.2    Fersht, A.R.3
  • 29
    • 0035459817 scopus 로고    scopus 로고
    • [Structure and function of calpain superfamily]
    • Hata S, Sorimachi H, Suzuki K, (2001) [Structure and function of calpain superfamily]. Seikagaku 73: 1129-1140.
    • (2001) Seikagaku , vol.73 , pp. 1129-1140
    • Hata, S.1    Sorimachi, H.2    Suzuki, K.3
  • 30
    • 0026066644 scopus 로고
    • Signal sequence-independent protein secretion in gram-negative bacteria: colicin V and microcin B17
    • Skvirsky RC, Gilson L, Kolter R, (1991) Signal sequence-independent protein secretion in gram-negative bacteria: colicin V and microcin B17. Methods Cell Biol 34: 205-221.
    • (1991) Methods Cell Biol , vol.34 , pp. 205-221
    • Skvirsky, R.C.1    Gilson, L.2    Kolter, R.3
  • 32
    • 0036120574 scopus 로고    scopus 로고
    • Mapping the rubella virus subgenomic promoter
    • Tzeng WP, Frey TK, (2002) Mapping the rubella virus subgenomic promoter. J Virol 76: 3189-3201.
    • (2002) J Virol , vol.76 , pp. 3189-3201
    • Tzeng, W.P.1    Frey, T.K.2
  • 33
  • 34
    • 0030858697 scopus 로고    scopus 로고
    • Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion protein family, interacts with CvaB and TolC
    • Hwang J, Zhong X, Tai PC, (1997) Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion protein family, interacts with CvaB and TolC. J Bacteriol 179: 6264-6270.
    • (1997) J Bacteriol , vol.179 , pp. 6264-6270
    • Hwang, J.1    Zhong, X.2    Tai, P.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.