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Volumn 179, Issue 2, 2012, Pages 211-221

Novel structural and functional insights into the MoxR family of AAA+ ATPases

Author keywords

ATPases; Cofactor insertion; MoxR; Protein complex formation; RavA; Stress response; Von Willebrand factor A domain

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CARBON MONOXIDE; MAGNESIUM; PROTEIN MOXR; UNCLASSIFIED DRUG;

EID: 84864380055     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.03.010     Document Type: Review
Times cited : (30)

References (41)
  • 1
    • 49249126658 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli
    • Alexopoulos E., Kanjee U., Snider J., Houry W.A., Pai E.F. Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli. Acta Crystallogr. Sect. F 2008, 64:700-706.
    • (2008) Acta Crystallogr. Sect. F , vol.64 , pp. 700-706
    • Alexopoulos, E.1    Kanjee, U.2    Snider, J.3    Houry, W.A.4    Pai, E.F.5
  • 2
    • 85006100782 scopus 로고
    • Hyper-autolysis of the faculatative alkaliphile Bacillus sp. C-125 cells grown at neutral pH: culture-pH dependent cross-linking of the peptide moieties of the peptidoglycan
    • Aono R., Sanada T. Hyper-autolysis of the faculatative alkaliphile Bacillus sp. C-125 cells grown at neutral pH: culture-pH dependent cross-linking of the peptide moieties of the peptidoglycan. Biosci. Biotechnol. Biochem. 1994, 58:2015-2019.
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 2015-2019
    • Aono, R.1    Sanada, T.2
  • 3
    • 0032952078 scopus 로고    scopus 로고
    • Effect of nitrogen oxides on expression of the nir and nor genes for denitrification in Pseudomonas aeruginosa
    • Arai H., Kodama T., Igarashi Y. Effect of nitrogen oxides on expression of the nir and nor genes for denitrification in Pseudomonas aeruginosa. FEMS Microbiol. Lett. 1999, 170:19-24.
    • (1999) FEMS Microbiol. Lett. , vol.170 , pp. 19-24
    • Arai, H.1    Kodama, T.2    Igarashi, Y.3
  • 4
    • 0030984912 scopus 로고    scopus 로고
    • Characterization of the nitric oxide reductase-encoding region in Rhodobacter sphaeroides 2.4.3
    • Bartnikas T.B., Tosques I.E., Laratta W.P., Shi J., Shapleigh J.P. Characterization of the nitric oxide reductase-encoding region in Rhodobacter sphaeroides 2.4.3. J. Bacteriol. 1997, 179:3534-3540.
    • (1997) J. Bacteriol. , vol.179 , pp. 3534-3540
    • Bartnikas, T.B.1    Tosques, I.E.2    Laratta, W.P.3    Shi, J.4    Shapleigh, J.P.5
  • 5
  • 7
    • 0030438017 scopus 로고    scopus 로고
    • Mutational analysis of the nor gene cluster which encodes nitric-oxide reductase from Paracoccus denitrificans
    • de Boer A.P., van der Oost J., Reijnders W.N., Westerhoff H.V., Stouthamer A.H., et al. Mutational analysis of the nor gene cluster which encodes nitric-oxide reductase from Paracoccus denitrificans. Eur. J. Biochem. 1996, 242:592-600.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 592-600
    • de Boer, A.P.1    van der Oost, J.2    Reijnders, W.N.3    Westerhoff, H.V.4    Stouthamer, A.H.5
  • 8
    • 79953324922 scopus 로고    scopus 로고
    • Identification of a putative chaperone involved in stress resistance and virulence in Francisella tularensis
    • Dieppedale J., Sobral D., Dupuis M., Dubail I., Klimentova J., et al. Identification of a putative chaperone involved in stress resistance and virulence in Francisella tularensis. Infect. Immun. 2011, 79:1428-1439.
    • (2011) Infect. Immun. , vol.79 , pp. 1428-1439
    • Dieppedale, J.1    Sobral, D.2    Dupuis, M.3    Dubail, I.4    Klimentova, J.5
  • 9
    • 0033529852 scopus 로고    scopus 로고
    • Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulphur flavoprotein containing S-selanylcysteine
    • Dobbek H., Gremer L., Meyer O., huber R. Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulphur flavoprotein containing S-selanylcysteine. PNAS 1999, 96:8884-8889.
    • (1999) PNAS , vol.96 , pp. 8884-8889
    • Dobbek, H.1    Gremer, L.2    Meyer, O.3    huber, R.4
  • 10
    • 6344275008 scopus 로고    scopus 로고
    • Calcium signalling in bacteria
    • Dominguez D.C. Calcium signalling in bacteria. Mol. Microbiol. 2004, 54:291-297.
    • (2004) Mol. Microbiol. , vol.54 , pp. 291-297
    • Dominguez, D.C.1
  • 11
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 12
    • 78651113305 scopus 로고    scopus 로고
    • Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity
    • El Bakkouri M., Gutsche I., Kanjee U., Zhao B., Yu M., et al. Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity. PNAS 2010, 107:22499-22504.
    • (2010) PNAS , vol.107 , pp. 22499-22504
    • El Bakkouri, M.1    Gutsche, I.2    Kanjee, U.3    Zhao, B.4    Yu, M.5
  • 13
    • 0035800571 scopus 로고    scopus 로고
    • Interplay between an AAA module and integrin I domain may regulate the function of magnesium chelatase
    • Fodje M.N., Hansson A., Hansson M., Olsen J.G., Gough S., et al. Interplay between an AAA module and integrin I domain may regulate the function of magnesium chelatase. J. Mol. Biol. 2001, 311:111-122.
    • (2001) J. Mol. Biol. , vol.311 , pp. 111-122
    • Fodje, M.N.1    Hansson, A.2    Hansson, M.3    Olsen, J.G.4    Gough, S.5
  • 15
    • 0015811630 scopus 로고
    • Mode of action of glycine on the biosynthesis of peptidoglycan
    • Hammes W., Schleifer K.H., Kandler O. Mode of action of glycine on the biosynthesis of peptidoglycan. J. Bacteriol. 1973, 116:1029-1053.
    • (1973) J. Bacteriol. , vol.116 , pp. 1029-1053
    • Hammes, W.1    Schleifer, K.H.2    Kandler, O.3
  • 16
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer L.M., Leipe D.D., Koonin E.V., Aravind L. Evolutionary history and higher order classification of AAA+ ATPases. J. Struct. Biol. 2004, 146:11-31.
    • (2004) J. Struct. Biol. , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 17
    • 0026620454 scopus 로고
    • Interdependence of respiratory NO reduction and nitrite reduction revealed by mutagenesis of nirQ, a novel gene in the denitrification gene cluster of Pseudomonas stutzeri
    • Jungst A., Zumft W.G. Interdependence of respiratory NO reduction and nitrite reduction revealed by mutagenesis of nirQ, a novel gene in the denitrification gene cluster of Pseudomonas stutzeri. FEBS Lett. 1992, 314:308-314.
    • (1992) FEBS Lett. , vol.314 , pp. 308-314
    • Jungst, A.1    Zumft, W.G.2
  • 18
    • 79952280501 scopus 로고    scopus 로고
    • Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase
    • Kanjee U., Gutsche I., Alexopoulos E., Zhao B., El Bakkouri M., et al. Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase. EMBO J. 2011, 30:931-944.
    • (2011) EMBO J. , vol.30 , pp. 931-944
    • Kanjee, U.1    Gutsche, I.2    Alexopoulos, E.3    Zhao, B.4    El Bakkouri, M.5
  • 19
    • 67650931139 scopus 로고    scopus 로고
    • Calcium leads to further increase in glycine-enhanced extracellular secretion of recombinant α-cyclodextrin glycosyltransferase in Escherichia coli
    • Li Z.F., Li B., Liu Z.G., Wang M., Gu Z.B., et al. Calcium leads to further increase in glycine-enhanced extracellular secretion of recombinant α-cyclodextrin glycosyltransferase in Escherichia coli. J. Agric. Food Chem. 2009, 57:6231-6237.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 6231-6237
    • Li, Z.F.1    Li, B.2    Liu, Z.G.3    Wang, M.4    Gu, Z.B.5
  • 20
    • 77649111713 scopus 로고    scopus 로고
    • ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase
    • Lundqvist J., Elmlund H., Wulff R.P., Berglund L., Elmlund D., et al. ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase. Structure 2010, 18:354-365.
    • (2010) Structure , vol.18 , pp. 354-365
    • Lundqvist, J.1    Elmlund, H.2    Wulff, R.P.3    Berglund, L.4    Elmlund, D.5
  • 21
    • 0026772547 scopus 로고
    • Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH
    • Meng S.Y., Bennett G.N. Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH. J. Bacteriol. 1992, 174:2659-2669.
    • (1992) J. Bacteriol. , vol.174 , pp. 2659-2669
    • Meng, S.Y.1    Bennett, G.N.2
  • 22
    • 0033789043 scopus 로고    scopus 로고
    • The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase
    • Meyer O., Gremer L., Ferner R., Ferner M., Dobbek H., et al. The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase. Biol. Chem. 2000, 381:865-876.
    • (2000) Biol. Chem. , vol.381 , pp. 865-876
    • Meyer, O.1    Gremer, L.2    Ferner, R.3    Ferner, M.4    Dobbek, H.5
  • 24
    • 9244230099 scopus 로고    scopus 로고
    • Stationary-phase physiology
    • Nystrom T. Stationary-phase physiology. Annu. Rev. Microbiol. 2004, 58:161-181.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 161-181
    • Nystrom, T.1
  • 25
    • 44649141367 scopus 로고    scopus 로고
    • Coordinating nodule morphogenesis with rhizobial infection in legumes
    • Oldroyd G.E.D., Downie J.A. Coordinating nodule morphogenesis with rhizobial infection in legumes. Ann. Rev. Plant Biol. 2008, 59:519-546.
    • (2008) Ann. Rev. Plant Biol. , vol.59 , pp. 519-546
    • Oldroyd, G.E.D.1    Downie, J.A.2
  • 27
    • 33745170394 scopus 로고    scopus 로고
    • Structural and genomic properties of the Hyperthermophilic Archaeal virus ATV with an extracellular stage of the reproductive cycle
    • Prangishvili D., Vestergaard G., Haring M., Aramayo R., Basta T., et al. Structural and genomic properties of the Hyperthermophilic Archaeal virus ATV with an extracellular stage of the reproductive cycle. J. Mol. Biol. 2006, 359:1203-1216.
    • (2006) J. Mol. Biol. , vol.359 , pp. 1203-1216
    • Prangishvili, D.1    Vestergaard, G.2    Haring, M.3    Aramayo, R.4    Basta, T.5
  • 28
    • 0015957627 scopus 로고
    • Purification and physical properties of inducible Escherichia coli lysine decarboxylase
    • Sabo D.L., Boeker E.A., Byers B., Waron H., Fischer E.H. Purification and physical properties of inducible Escherichia coli lysine decarboxylase. Biochemistry (Mosc) 1974, 13:662-670.
    • (1974) Biochemistry (Mosc) , vol.13 , pp. 662-670
    • Sabo, D.L.1    Boeker, E.A.2    Byers, B.3    Waron, H.4    Fischer, E.H.5
  • 29
    • 77649222032 scopus 로고    scopus 로고
    • Cell biology and molecular ecology of Francisella tularensis
    • Santic M., Al-khodor S., Kwaik Y.A. Cell biology and molecular ecology of Francisella tularensis. Cell. Microbiol. 2010, 12:129-139.
    • (2010) Cell. Microbiol. , vol.12 , pp. 129-139
    • Santic, M.1    Al-khodor, S.2    Kwaik, Y.A.3
  • 30
    • 79955447193 scopus 로고    scopus 로고
    • Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus ATV
    • Scheele U., Erdmann S., Ungewickell E.J., Felisberto-Rodrigues C., Ortiz-Lombardia M., et al. Chaperone role for proteins p618 and p892 in the extracellular tail development of Acidianus two-tailed virus ATV. J. Virol. 2011, 85:4812-4821.
    • (2011) J. Virol. , vol.85 , pp. 4812-4821
    • Scheele, U.1    Erdmann, S.2    Ungewickell, E.J.3    Felisberto-Rodrigues, C.4    Ortiz-Lombardia, M.5
  • 31
    • 65149084160 scopus 로고    scopus 로고
    • The AAA+ superfamily of functionally diverse proteins
    • Snider J., Thibault G., Houry W.A. The AAA+ superfamily of functionally diverse proteins. Genome Biol. 2008, 9:216.
    • (2008) Genome Biol. , vol.9 , pp. 216
    • Snider, J.1    Thibault, G.2    Houry, W.A.3
  • 32
    • 33749337533 scopus 로고    scopus 로고
    • MoxR AAA+ ATPases: a novel family of molecular chaperones?
    • Snider J.D., Houry W.A. MoxR AAA+ ATPases: a novel family of molecular chaperones?. J. Struct. Biol. 2006, 156:200-209.
    • (2006) J. Struct. Biol. , vol.156 , pp. 200-209
    • Snider, J.D.1    Houry, W.A.2
  • 33
    • 33644982684 scopus 로고    scopus 로고
    • Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase
    • Snider J.D., Gutsche I., Lin M., Baby S., Cox B., et al. Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase. J. Biol. Chem. 2006, 281:1532-1546.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1532-1546
    • Snider, J.D.1    Gutsche, I.2    Lin, M.3    Baby, S.4    Cox, B.5
  • 34
    • 33846213195 scopus 로고    scopus 로고
    • Complement and the multifaceted functions of VWA and integrin I domains
    • Springer T.A. Complement and the multifaceted functions of VWA and integrin I domains. Structure 2006, 14:11-16.
    • (2006) Structure , vol.14 , pp. 11-16
    • Springer, T.A.1
  • 35
    • 0032589120 scopus 로고    scopus 로고
    • Characterization of the BatI (Bacteroides aerotolerance) operon in Bacteroides fragilis: isolation of a B. fragilis mutant with reduced aerotolerance and impaired growth in in vivo model systems
    • Tang Y.P., Dallas M.M., Malamy M.H. Characterization of the BatI (Bacteroides aerotolerance) operon in Bacteroides fragilis: isolation of a B. fragilis mutant with reduced aerotolerance and impaired growth in in vivo model systems. Mol. Microbiol. 1999, 32:139-149.
    • (1999) Mol. Microbiol. , vol.32 , pp. 139-149
    • Tang, Y.P.1    Dallas, M.M.2    Malamy, M.H.3
  • 36
    • 0031691347 scopus 로고    scopus 로고
    • Construction of insertion and deletion mxa mutants of Methylobacterium extorquens AM1 by electroporation
    • Toyama H., Anthony C., Lidstrom M.E. Construction of insertion and deletion mxa mutants of Methylobacterium extorquens AM1 by electroporation. FEMS Microbiol. Lett. 1998, 166:1-7.
    • (1998) FEMS Microbiol. Lett. , vol.166 , pp. 1-7
    • Toyama, H.1    Anthony, C.2    Lidstrom, M.E.3
  • 37
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara M. Agents that increase the permeability of the outer membrane. Microbiol. Rev. 1992, 56:395-411.
    • (1992) Microbiol. Rev. , vol.56 , pp. 395-411
    • Vaara, M.1
  • 38
    • 0025885443 scopus 로고
    • Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth
    • van Spanning R.J., Wansell C.W., de Boer T., Hazelaar M.J., Anazawa H., et al. Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth. J. Bacteriol. 1991, 173:6948-6961.
    • (1991) J. Bacteriol. , vol.173 , pp. 6948-6961
    • van Spanning, R.J.1    Wansell, C.W.2    de Boer, T.3    Hazelaar, M.J.4    Anazawa, H.5
  • 39
    • 79958122911 scopus 로고    scopus 로고
    • Mutation of a broadly conserved operon (RL3499-RL3502) from Rhizobium leguminosarum biovar viciae causes defects in cell morphology and envelope integrity
    • Vanderlinde E.M., Magnus S.A., Tambalo D.D., Koval S.F., Yost C.K. Mutation of a broadly conserved operon (RL3499-RL3502) from Rhizobium leguminosarum biovar viciae causes defects in cell morphology and envelope integrity. J. Bacteriol. 2011, 193:2684-2694.
    • (2011) J. Bacteriol. , vol.193 , pp. 2684-2694
    • Vanderlinde, E.M.1    Magnus, S.A.2    Tambalo, D.D.3    Koval, S.F.4    Yost, C.K.5
  • 40
    • 0035096082 scopus 로고    scopus 로고
    • Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism
    • Wang J., Song J.J., Franklin M.C., Kamtekar S., Im Y.J., et al. Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. Structure 2001, 9:177-184.
    • (2001) Structure , vol.9 , pp. 177-184
    • Wang, J.1    Song, J.J.2    Franklin, M.C.3    Kamtekar, S.4    Im, Y.J.5
  • 41
    • 0036796740 scopus 로고    scopus 로고
    • Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere
    • Whittaker C.A., Hynes R.O. Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. Mol. Biol. Cell 2002, 13:3369-3387.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2


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