메뉴 건너뛰기




Volumn 11, Issue 3-5, 2006, Pages 167-191

Archaeal flagella, bacterial flagella and type IV pili: A comparison of genes and posttranslational modifications

Author keywords

Archaeal flagella; Bacterial flagella; Flagellar gene families; Flagellin pilin subunit glycosylation; Genes and posttranslational modifications, a comparison; Preflagellin prepilin signal peptide processing; Type IV pili

Indexed keywords

PEPTIDASE;

EID: 33748757929     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: 10.1159/000094053     Document Type: Review
Times cited : (107)

References (139)
  • 1
    • 0030023488 scopus 로고    scopus 로고
    • Flagella assembly in Salmonella typhimurium
    • Aizawa SI: Flagella assembly in Salmonella typhimurium. Mol Microbiol 1996;19:1-5.
    • (1996) Mol Microbiol , vol.19 , pp. 1-5
    • Aizawa, S.I.1
  • 2
    • 0038170287 scopus 로고    scopus 로고
    • Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity
    • Albers SV, Szabo Z, Driessen AJM: Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity. J Bacteriol 2003;185:3918-3925.
    • (2003) J Bacteriol , vol.185 , pp. 3918-3925
    • Albers, S.V.1    Szabo, Z.2    Driessen, A.J.M.3
  • 4
    • 0030907570 scopus 로고    scopus 로고
    • Genes involved in the biogenesis and function of type-4 fimbriae in Pseudomonas aeruginosa
    • Alm RA, Mattick JS: Genes involved in the biogenesis and function of type-4 fimbriae in Pseudomonas aeruginosa. Gene 1997;192:89-98.
    • (1997) Gene , vol.192 , pp. 89-98
    • Alm, R.A.1    Mattick, J.S.2
  • 5
    • 0033277365 scopus 로고    scopus 로고
    • Bacterial tactic responses
    • Armitage JP: Bacterial tactic responses. Adv Microb Physiol 1999;41:229-289.
    • (1999) Adv Microb Physiol , vol.41 , pp. 229-289
    • Armitage, J.P.1
  • 6
    • 0035979193 scopus 로고    scopus 로고
    • A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation
    • Arora SK, Bangera M, Lory S, Ramphal R: A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation. Proc Natl Acad Sci USA 2001;98:9342-9347.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9342-9347
    • Arora, S.K.1    Bangera, M.2    Lory, S.3    Ramphal, R.4
  • 7
    • 1642300392 scopus 로고    scopus 로고
    • Sequence polymorphism in the glycosylation island and flagellins of Pseudomonas aeruginosa
    • Arora SK, Wolfgang MC, Lory S, Ramphal R: Sequence polymorphism in the glycosylation island and flagellins of Pseudomonas aeruginosa. J Bacteriol 2004;186:2115-2122.
    • (2004) J Bacteriol , vol.186 , pp. 2115-2122
    • Arora, S.K.1    Wolfgang, M.C.2    Lory, S.3    Ramphal, R.4
  • 8
    • 0018419825 scopus 로고
    • Methanogens: Reevaluation of a unique biological group
    • Balch WE, Fox GE, Woese CR, Wolfe RS: Methanogens: reevaluation of a unique biological group. Microbiol Rev 1979;43:260-296.
    • (1979) Microbiol Rev , vol.43 , pp. 260-296
    • Balch, W.E.1    Fox, G.E.2    Woese, C.R.3    Wolfe, R.S.4
  • 9
    • 0037133374 scopus 로고    scopus 로고
    • FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity
    • Bardy SL, Jarrell KF: FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity. FEMS Microbiol Lett 2002;208:53-59.
    • (2002) FEMS Microbiol Lett , vol.208 , pp. 53-59
    • Bardy, S.L.1    Jarrell, K.F.2
  • 10
    • 0345257806 scopus 로고    scopus 로고
    • Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae
    • Bardy SL, Jarrell KF: Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae. Mol Microbiol 2003;50:1339-1347.
    • (2003) Mol Microbiol , vol.50 , pp. 1339-1347
    • Bardy, S.L.1    Jarrell, K.F.2
  • 11
    • 0036777348 scopus 로고    scopus 로고
    • Identification and localization of flagellins FlaA and FlaB3 within the flagella of Methanococcus voltae
    • Bardy SL, Mori T, Komoriya K, Aizawa SI, Jarrell KF: Identification and localization of flagellins FlaA and FlaB3 within the flagella of Methanococcus voltae. J Bacteriol 2002;184:5223-5233.
    • (2002) J Bacteriol , vol.184 , pp. 5223-5233
    • Bardy, S.L.1    Mori, T.2    Komoriya, K.3    Aizawa, S.I.4    Jarrell, K.F.5
  • 12
    • 0043013091 scopus 로고    scopus 로고
    • Archaeal signal peptides - A comparative survey at the genome level
    • Bardy SL, Eichler J, Jarrell KF: Archaeal signal peptides - a comparative survey at the genome level. Prot Sci 2003;12:1833-1843.
    • (2003) Prot Sci , vol.12 , pp. 1833-1843
    • Bardy, S.L.1    Eichler, J.2    Jarrell, K.F.3
  • 13
    • 2642553801 scopus 로고    scopus 로고
    • Recent advances in the structure and assembly of the archaeal flagellum
    • Bardy SL, Ng SY, Jarrell KF: Recent advances in the structure and assembly of the archaeal flagellum. J Mol Microbiol Biotechnol 2004;7:41-51.
    • (2004) J Mol Microbiol Biotechnol , vol.7 , pp. 41-51
    • Bardy, S.L.1    Ng, S.Y.2    Jarrell, K.F.3
  • 14
    • 0032014974 scopus 로고    scopus 로고
    • Further evidence to suggest that archaeal flagella are related to bacterial type IV pili
    • Bayley DP, Jarrell KF: Further evidence to suggest that archaeal flagella are related to bacterial type IV pili. J Mol Evol 1998;46:370-373.
    • (1998) J Mol Evol , vol.46 , pp. 370-373
    • Bayley, D.P.1    Jarrell, K.F.2
  • 15
    • 0027328925 scopus 로고
    • Effect of bacitracin on flagellar assumbly and presumed glycosylation of the flagellins of Methanococcus deltae
    • Bayley DP, Kalmokoff ML, Jarrell KF: Effect of bacitracin on flagellar assumbly and presumed glycosylation of the flagellins of Methanococcus deltae. Arch Microbiol 1993;160:179-185.
    • (1993) Arch Microbiol , vol.160 , pp. 179-185
    • Bayley, D.P.1    Kalmokoff, M.L.2    Jarrell, K.F.3
  • 16
    • 0031872760 scopus 로고    scopus 로고
    • Flagellin genes of Methanococcus vannielii: Amplification by the polymerase chain reaction, demonstration of signal peptides and identification of major components of the flagellar filament
    • Bayley DP, Florian V, Klein A, Jarrell KF: Flagellin genes of Methanococcus vannielii: amplification by the polymerase chain reaction, demonstration of signal peptides and identification of major components of the flagellar filament. Mol Gen Genet 1998;258:639-645.
    • (1998) Mol Gen Genet , vol.258 , pp. 639-645
    • Bayley, D.P.1    Florian, V.2    Klein, A.3    Jarrell, K.F.4
  • 17
    • 0036067107 scopus 로고    scopus 로고
    • Never say never again: Protein glycosylation in pathogenic bacteria
    • Benz I, Schmidt MA: Never say never again: protein glycosylation in pathogenic bacteria. Mol Microbiol 2002;45:267-276.
    • (2002) Mol Microbiol , vol.45 , pp. 267-276
    • Benz, I.1    Ma, S.2
  • 18
    • 0037615052 scopus 로고    scopus 로고
    • Secretins of Pseudomonas aeruginosa: Large holes in the outer membrane
    • Bitter W: Secretins of Pseudomonas aeruginosa: large holes in the outer membrane. Arch Microbiol 2003;179:307-314.
    • (2003) Arch Microbiol , vol.179 , pp. 307-314
    • Bitter, W.1
  • 19
    • 0031983616 scopus 로고    scopus 로고
    • Formation ofoligomeric rings by XcpQ and PiIQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa
    • Bitter W, Koster M, Latijnhouwers M, de Cock H, Tommassen J: Formation ofoligomeric rings by XcpQ and PiIQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa. Mol Microbiol 1998;27:209-219.
    • (1998) Mol Microbiol , vol.27 , pp. 209-219
    • Bitter, W.1    Koster, M.2    Latijnhouwers, M.3    De Cock, H.4    Tommassen, J.5
  • 20
    • 77957231504 scopus 로고
    • Biosynthesis of O-glycans of the N-acetylgalactosamine-α-Ser/Thr linkage type
    • Montreuil J, Schachter H, Vliegenthart JFG (eds): New York, Elsevier Science
    • Brockhausen I: Biosynthesis of O-glycans of the N-acetylgalactosamine- α-Ser/Thr linkage type; in Montreuil J, Schachter H, Vliegenthart JFG (eds): Glycoprotein. New York, Elsevier Science, 1995, pp 201-259.
    • (1995) Glycoprotein , pp. 201-259
    • Brockhausen, I.1
  • 21
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of N-linked glycosylation
    • Burda P, Aebi M: The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta 1999;1426:694-708.
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 694-708
    • Burda, P.1    Aebi, M.2
  • 22
    • 0035854812 scopus 로고    scopus 로고
    • Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan
    • Gastric P, Cassels FJ, Carlson RW: Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan. J Biol Chem 2001;276:26479-26485.
    • (2001) J Biol Chem , vol.276 , pp. 26479-26485
    • Gastric, P.1    Cassels, F.J.2    Carlson, R.W.3
  • 23
    • 33745207351 scopus 로고    scopus 로고
    • Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: Insight into N-linked glycosylation pathways in Archaea
    • Chaban B, Voisin S, Kelly J, Logan SM; Jarrell KF: Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea. Mol Microbiol 2006;61:259-268.
    • (2006) Mol Microbiol , vol.61 , pp. 259-268
    • Chaban, B.1    Voisin, S.2    Kelly, J.3    Logan, S.M.4    Jarrell, K.F.5
  • 24
    • 0034444676 scopus 로고    scopus 로고
    • Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar Typhimurium and Escherichia coli
    • Chilcott GS, Hughes KT: Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar Typhimurium and Escherichia coli. Microbiol Mol Biol Rev 2000;64:694-708.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 694-708
    • Chilcott, G.S.1    Hughes, K.T.2
  • 25
    • 0038460046 scopus 로고    scopus 로고
    • Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly
    • Claret L, Calder SR, Higgins M, Hughes C: Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly. Mol Microbiol 2003;48:1349-1355.
    • (2003) Mol Microbiol , vol.48 , pp. 1349-1355
    • Claret, L.1    Calder, S.R.2    Higgins, M.3    Hughes, C.4
  • 26
    • 0036384351 scopus 로고    scopus 로고
    • The structure of the archaebacterial flagellar filament of the extreme halophile Halobacterium salinarum R1M1 and its relation to eubacterial flagellar filaments and type IV pili
    • Cohen-Krausz S, Trachtenberg S: The structure of the archaebacterial flagellar filament of the extreme halophile Halobacterium salinarum R1M1 and its relation to eubacterial flagellar filaments and type IV pili. J Mol Biol 2002;321:383-395.
    • (2002) J Mol Biol , vol.321 , pp. 383-395
    • Cohen-Krausz, S.1    Trachtenberg, S.2
  • 27
    • 0033958226 scopus 로고    scopus 로고
    • Posttranslational processing of Methanococcus voltae preflagellin by preflagellin peptidases of M. voltae and other methanogens
    • Correia JD, Jarrell KF: Posttranslational processing of Methanococcus voltae preflagellin by preflagellin peptidases of M. voltae and other methanogens. J Bacteriol 2000;182:855-858.
    • (2000) J Bacteriol , vol.182 , pp. 855-858
    • Correia, J.D.1    Jarrell, K.F.2
  • 29
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • Craig L, Pique ME, Tainer JA: Type IV pilus structure and bacterial pathogenicity. Nat Rev Microbiol 2004;2:363-378.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 30
    • 1942424083 scopus 로고    scopus 로고
    • The inner membrane subassembly of the enteropathogenic Escherichia coli bundle-forming pilus machine
    • Crowther LJ, Anantha RP, Donnenberg MS: The inner membrane subassembly of the enteropathogenic Escherichia coli bundle-forming pilus machine. Mol Microbiol 2004;52:67-79.
    • (2004) Mol Microbiol , vol.52 , pp. 67-79
    • Crowther, L.J.1    Anantha, R.P.2    Donnenberg, M.S.3
  • 31
    • 0024333288 scopus 로고
    • Isolation and ultrastructure of the flagella of Methanococcus thermolithotrophicus and Methanospirillum hungatei
    • Cruden D, Sparling R, Markovetz AJ: Isolation and ultrastructure of the flagella of Methanococcus thermolithotrophicus and Methanospirillum hungatei. App Environ Microbiol 1989;55:1414-1419.
    • (1989) App Environ Microbiol , vol.55 , pp. 1414-1419
    • Cruden, D.1    Sparling, R.2    Markovetz, A.J.3
  • 32
    • 0028339637 scopus 로고
    • Characterization of a Pseudomonas aeruginosa gene cluster involved in pilus biosynthesis and twitching motility: Sequence similarity to the chemotaxis proteins of enterics and the gliding bacterium Myxococcus xanthus
    • Darzins A: Characterization of a Pseudomonas aeruginosa gene cluster involved in pilus biosynthesis and twitching motility: sequence similarity to the chemotaxis proteins of enterics and the gliding bacterium Myxococcus xanthus. Mol Microbiol 1994;11:137-153.
    • (1994) Mol Microbiol , vol.11 , pp. 137-153
    • Darzins, A.1
  • 34
    • 0030049732 scopus 로고    scopus 로고
    • Characterization of a posttranslational modification of Campylobacter flagellin: Identification of a sero-specific glycosyl moiety
    • Doig P, Kinsella N, Guerry P, Trust TJ: Characterization of a posttranslational modification of Campylobacter flagellin: identification of a sero-specific glycosyl moiety. Mol Microbiol 1996;19:379-387.
    • (1996) Mol Microbiol , vol.19 , pp. 379-387
    • Doig, P.1    Kinsella, N.2    Guerry, P.3    Trust, T.J.4
  • 35
    • 0031006045 scopus 로고    scopus 로고
    • Biogenesis of the bundle-forming pilus of enteropathogenic Escherichia coli: Reconstitution of fimbriae in recombinant E. coli and role of DsbA in pilin stability - A review
    • Donnenberg MS, Zhang HZ, Stone KD: Biogenesis of the bundle-forming pilus of enteropathogenic Escherichia coli: reconstitution of fimbriae in recombinant E. coli and role of DsbA in pilin stability - a review. Gene 1997;192:33-38.
    • (1997) Gene , vol.192 , pp. 33-38
    • Donnenberg, M.S.1    Zhang, H.Z.2    Stone, K.D.3
  • 36
    • 0037406829 scopus 로고    scopus 로고
    • Type II protein secretion in Pseudomonas aeruginosa: The pseudopilus is a multifibrillar and adhesive structure
    • Durand E, Bernadac A, Ball G, Lazdunski A, Sturgis JN, Filloux A: Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure. J Bacteriol 2003;185:279-281.
    • (2003) J Bacteriol , vol.185 , pp. 279-281
    • Durand, E.1    Bernadac, A.2    Ball, G.3    Lazdunski, A.4    Sturgis, J.N.5    Filloux, A.6
  • 37
    • 0033040340 scopus 로고    scopus 로고
    • A twisted tale: The origin and evolution of motility and chemotaxis in prokaryotes
    • Faguy DM, Jarrell KF: A twisted tale: the origin and evolution of motility and chemotaxis in prokaryotes. Microbiology 1999;145:279-281.
    • (1999) Microbiology , vol.145 , pp. 279-281
    • Faguy, D.M.1    Jarrell, K.F.2
  • 38
    • 0028182415 scopus 로고
    • Molecular analysis of archaeal flagellins: Similarity to the type IV pilin-transport superfamily widespread in bacteria
    • Faguy DM, Jarrell KF, Kuzio J, Kalmokoff ML: Molecular analysis of archaeal flagellins: similarity to the type IV pilin-transport superfamily widespread in bacteria. Can J Microbiol 1994;40:67-71.
    • (1994) Can J Microbiol , vol.40 , pp. 67-71
    • Faguy, D.M.1    Jarrell, K.F.2    Kuzio, J.3    Kalmokoff, M.L.4
  • 39
    • 0030058179 scopus 로고    scopus 로고
    • Isolation and characterization of flagella and flagellin proteins from the thermoacidophilic archaea Thermoplasma volcanium and Sulfolobus shibatae
    • Faguy DM, Bayley DP, Kostyukova AS, Thomas NA, Jarrell KF: Isolation and characterization of flagella and flagellin proteins from the thermoacidophilic archaea Thermoplasma volcanium and Sulfolobus shibatae. J Bacteriol 1996;178:902-905.
    • (1996) J Bacteriol , vol.178 , pp. 902-905
    • Faguy, D.M.1    Bayley, D.P.2    Kostyukova, A.S.3    Thomas, N.A.4    Jarrell, K.F.5
  • 41
    • 0019494384 scopus 로고
    • Structure of polar pili from Pseudomonas aeruginosa strains K and O
    • Folkhard W, Marvin DA, Watts TH, Paranchych W: Structure of polar pili from Pseudomonas aeruginosa strains K and O. J Mol Biol 1981;149:79-93.
    • (1981) J Mol Biol , vol.149 , pp. 79-93
    • Folkhard, W.1    Marvin, D.A.2    Watts, T.H.3    Paranchych, W.4
  • 42
    • 0032905128 scopus 로고    scopus 로고
    • Crystallographic structure reveals phosphorylated pilin from Neisseria: Phosphoserine sites modify type IV pilus surface chemistry and fibre morphology
    • Forest KT, Dunham SA, Koomey M, Tainer JA: Crystallographic structure reveals phosphorylated pilin from Neisseria: phosphoserine sites modify type IV pilus surface chemistry and fibre morphology. Mol Microbiol 1999;31:743-752.
    • (1999) Mol Microbiol , vol.31 , pp. 743-752
    • Forest, K.T.1    Dunham, S.A.2    Koomey, M.3    Tainer, J.A.4
  • 44
    • 0026740392 scopus 로고
    • Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body
    • Francis NR, Irikura VM, Yamaguchi S, DeRosier DJ: Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body. Proc Natl Acad Sci USA 1992;89:6304-6308.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6304-6308
    • Francis, N.R.1    Irikura, V.M.2    Yamaguchi, S.3    Derosier, D.J.4
  • 45
    • 0017407961 scopus 로고    scopus 로고
    • Composition and molecular weight of pili purified from Pseudomonas aeruginosa K
    • Frost LS, Paranchych W: Composition and molecular weight of pili purified from Pseudomonas aeruginosa K. J Bacteriol 1997;131:259-269.
    • (1997) J Bacteriol , vol.131 , pp. 259-269
    • Frost, L.S.1    Paranchych, W.2
  • 46
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel Y, von Heijne G: Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng 1990;3:433-442.
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 48
    • 17144438252 scopus 로고    scopus 로고
    • Ferroplasma acidiphilum gen. nov., sp. nov., an acidophilic, autotrophic, ferrous-iron-oxidizing, cell-wall-lacking, mesophilic member of the Ferroplasmaceae fam. nov., comprising a distinct lineage of the Archaea
    • Golyshina OV, Pivovarova TA, Karavaiko GI, Kondrateva TF, Moore ER, Abraham WR, Lunsdorf H, Timmis KN, Yakimov MM, Golyshin PN: Ferroplasma acidiphilum gen. nov., sp. nov., an acidophilic, autotrophic, ferrous-iron-oxidizing, cell-wall-lacking, mesophilic member of the Ferroplasmaceae fam. nov., comprising a distinct lineage of the Archaea. Int J Syst Evol Microbiol 2000;50:997-1006.
    • (2000) Int J Syst Evol Microbiol , vol.50 , pp. 997-1006
    • Golyshina, O.V.1    Pivovarova, T.A.2    Karavaiko, G.I.3    Kondrateva, T.F.4    Moore, E.R.5    Abraham, W.R.6    Lunsdorf, H.7    Timmis, K.N.8    Yakimov, M.M.9    Golyshin, P.N.10
  • 49
    • 0036041918 scopus 로고    scopus 로고
    • Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway
    • Gonzalez-Pedrajo B, Fraser GM, Minamino T, MacNab RM: Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway. Mol Microbiol 2002;45:967-982.
    • (2002) Mol Microbiol , vol.45 , pp. 967-982
    • Gonzalez-Pedrajo, B.1    Fraser, G.M.2    Minamino, T.3    MacNab, R.M.4
  • 50
    • 0142030034 scopus 로고    scopus 로고
    • Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene
    • Goon S, Kelly JF, Logan SM, Ewing CP, Guerry P: Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene. Mol Microbiol 2003;50:659-671.
    • (2003) Mol Microbiol , vol.50 , pp. 659-671
    • Goon, S.1    Kelly, J.F.2    Logan, S.M.3    Ewing, C.P.4    Guerry, P.5
  • 51
    • 12544251532 scopus 로고    scopus 로고
    • Halobacterium noricense sp. nov., an archaeal isolate from a bore core of an alpine Permina salt deposit, classification of Halobacterium sp. NRC-1 as a strain of H. salinarum and emended description of H. salinarum
    • Gruber C, Legat A, Pfaffenhuemer M, Radax C, Weidler G, Busse H-J, Stan-Lotter H: Halobacterium noricense sp. nov., an archaeal isolate from a bore core of an alpine Permina salt deposit, classification of Halobacterium sp. NRC-1 as a strain of H. salinarum and emended description of H. salinarum. Extremophiles 2004;8:431-439.
    • (2004) Extremophiles , vol.8 , pp. 431-439
    • Gruber, C.1    Legat, A.2    Pfaffenhuemer, M.3    Radax, C.4    Weidler, G.5    Busse, H.-J.6    Stan-Lotter, H.7
  • 53
    • 0029411457 scopus 로고
    • The type IV pre-pilin leader peptidase of Xanthomonas campestris pv. campestris is functional without conserved cysteine residues
    • Hu NT, Lee PF, Chen C: The type IV pre-pilin leader peptidase of Xanthomonas campestris pv. campestris is functional without conserved cysteine residues. Mol Microbiol 1995;18:769-777.
    • (1995) Mol Microbiol , vol.18 , pp. 769-777
    • Hu, N.T.1    Lee, P.F.2    Chen, C.3
  • 54
    • 0345097587 scopus 로고    scopus 로고
    • FimX, a multidomain protein connecting environmental signals to twitching motility in Pseudomonas aeruginosa
    • Huang B, Whitchurch CB, Mattick JS: FimX, a multidomain protein connecting environmental signals to twitching motility in Pseudomonas aeruginosa. J Bacteriol 2003;185:7068-7076.
    • (2003) J Bacteriol , vol.185 , pp. 7068-7076
    • Huang, B.1    Whitchurch, C.B.2    Mattick, J.S.3
  • 55
    • 0242575007 scopus 로고    scopus 로고
    • Structural and topographical studies of the type IV bundle-forming pilus assembly complex of enteropathogenic Escherichia coli
    • Hwang J, Bieber D, Ramer SW, Wu CY, Schoolnik GK: Structural and topographical studies of the type IV bundle-forming pilus assembly complex of enteropathogenic Escherichia coli. J Bacteriol 2003;185:6695-6701.
    • (2003) J Bacteriol , vol.185 , pp. 6695-6701
    • Hwang, J.1    Bieber, D.2    Ramer, S.W.3    Wu, C.Y.4    Schoolnik, G.K.5
  • 56
    • 0014515268 scopus 로고
    • Polarity of flagellar growth in Salmonella
    • Iino T: Polarity of flagellar growth in Salmonella. J Gen Microbiol 1969;56:227-239.
    • (1969) J Gen Microbiol , vol.56 , pp. 227-239
    • Iino, T.1
  • 57
    • 0029881205 scopus 로고    scopus 로고
    • Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae
    • Jarrell KF, Bayley DP, Florian V, Klein A: Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae. Mol Microbiol 1996;20:657-666.
    • (1996) Mol Microbiol , vol.20 , pp. 657-666
    • Jarrell, K.F.1    Bayley, D.P.2    Florian, V.3    Klein, A.4
  • 58
    • 0027947083 scopus 로고
    • Imaging flagella of halobacteria by atomic force microscopy
    • Jaschke M, Butt H-J, Wolff EK: Imaging flagella of halobacteria by atomic force microscopy. Analyst 1994;119:1943-1946.
    • (1994) Analyst , vol.119 , pp. 1943-1946
    • Jaschke, M.1    Butt, H.-J.2    Wolff, E.K.3
  • 59
    • 0025879107 scopus 로고
    • The bacterial flagellum and flagellar motor: Structure, assembly and function
    • Jones CJ, Aizawa S: The bacterial flagellum and flagellar motor: structure, assembly and function. Adv Microb Physiol 1991;32:109-172.
    • (1991) Adv Microb Physiol , vol.32 , pp. 109-172
    • Jones, C.J.1    Aizawa, S.2
  • 60
    • 0035449036 scopus 로고    scopus 로고
    • Genes for tight adherence of Actinobacillus actinomycetemcomitans: From plaque to plague to pond scum
    • Kachlany S, Planet P, DeSalle R, Fine D, Figurski D: Genes for tight adherence of Actinobacillus actinomycetemcomitans: from plaque to plague to pond scum. Trends Microbiol 2001;9:429-437.
    • (2001) Trends Microbiol , vol.9 , pp. 429-437
    • Kachlany, S.1    Planet, P.2    DeSalle, R.3    Fine, D.4    Figurski, D.5
  • 61
    • 0034597550 scopus 로고    scopus 로고
    • Bacterial motility: How do pili pull?
    • Kaiser D: Bacterial motility: how do pili pull? Curr Biol 2000;10:R777-R780.
    • (2000) Curr Biol , vol.10
    • Kaiser, D.1
  • 62
    • 0025833831 scopus 로고
    • Cloning and sequencing of a multigene family encoding the flagellins of Methanococcus voltae
    • Kalmokoff ML, Jarrell KF: Cloning and sequencing of a multigene family encoding the flagellins of Methanococcus voltae. J Bacteriol 1991;173:7113-7125.
    • (1991) J Bacteriol , vol.173 , pp. 7113-7125
    • Kalmokoff, M.L.1    Jarrell, K.F.2
  • 63
    • 0023990563 scopus 로고
    • Isolation of flagella from the archaebacterium Methanococcus voltae by phase separation with Triton X-114
    • Kalmokoff ML, Jarrell KF, Koval SF: Isolation of flagella from the archaebacterium Methanococcus voltae by phase separation with Triton X-114. J Bacteriol 1988;170:1752-1758.
    • (1988) J Bacteriol , vol.170 , pp. 1752-1758
    • Kalmokoff, M.L.1    Jarrell, K.F.2    Koval, S.F.3
  • 65
    • 0027166699 scopus 로고
    • Tyrosine phosphate in a- and b-type flagellins of Pseudomonas aeruginosa
    • Kelly-Wintenberg K, South SL, Montie TC: Tyrosine phosphate in a- and b-type flagellins of Pseudomonas aeruginosa. J Bacteriol 1993;175:2458-2461.
    • (1993) J Bacteriol , vol.175 , pp. 2458-2461
    • Kelly-Wintenberg, K.1    South, S.L.2    Montie, T.C.3
  • 67
    • 0037093395 scopus 로고    scopus 로고
    • A novel mode of sensory transduction in archaea: Binding protein-mediated chemotaxis towards osmoprotectants and amino acids
    • Kokoeva MV, Storch KF, Klein C, Oesterhelt D: A novel mode of sensory transduction in archaea: binding protein-mediated chemotaxis towards osmoprotectants and amino acids. EMBO J 2002;21:2312-2322.
    • (2002) EMBO J , vol.21 , pp. 2312-2322
    • Kokoeva, M.V.1    Storch, K.F.2    Klein, C.3    Oesterhelt, D.4
  • 68
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer ELL: Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J Mol Biol 2001;305:567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 69
    • 0028142579 scopus 로고
    • The flagellar bundle of Halobacterium salinarium is inserted into a distinct polar cap structure
    • Kupper J, Marwan W, Typke D, Grunberg H, Uwer U, Gluch M, Oesterhelt D: The flagellar bundle of Halobacterium salinarium is inserted into a distinct polar cap structure. J Bacteriol 1994;176:5184-5187.
    • (1994) J Bacteriol , vol.176 , pp. 5184-5187
    • Kupper, J.1    Marwan, W.2    Typke, D.3    Grunberg, H.4    Uwer, U.5    Gluch, M.6    Oesterhelt, D.7
  • 71
    • 0033978638 scopus 로고    scopus 로고
    • The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases
    • LaPointe CF, Taylor RK: The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases. J Biol Chem 2000;275:1502-1510.
    • (2000) J Biol Chem , vol.275 , pp. 1502-1510
    • LaPointe, C.F.1    Taylor, R.K.2
  • 72
    • 0024346543 scopus 로고
    • Structure and biosynthesis of prokaryotic glycoproteins
    • Lechner J, Wieland F: Structure and biosynthesis of prokaryotic glycoproteins. Annu Rev Biochem 1989;58:173-194.
    • (1989) Annu Rev Biochem , vol.58 , pp. 173-194
    • Lechner, J.1    Wieland, F.2
  • 73
    • 2642514676 scopus 로고    scopus 로고
    • The periplasmic flagellum of spirochetes
    • Limberger RJ: The periplasmic flagellum of spirochetes. J Mol Microbiol Biotechnol 2004;7:30-40.
    • (2004) J Mol Microbiol Biotechnol , vol.7 , pp. 30-40
    • Limberger, R.J.1
  • 74
    • 0032698478 scopus 로고    scopus 로고
    • The bacterial flagellum: Reversible rotary propellor and type III export apparatus
    • Macnab RM: The bacterial flagellum: reversible rotary propellor and type III export apparatus. J Bacteriol 1999;181:7149-7153.
    • (1999) J Bacteriol , vol.181 , pp. 7149-7153
    • Macnab, R.M.1
  • 75
    • 0026062036 scopus 로고
    • Rotation and switching of the flagellar motor assembly in Halobacterium halobium
    • Marwan W, Alam M, Oesterhelt D: Rotation and switching of the flagellar motor assembly in Halobacterium halobium. J Bacteriol 1991;173:1971-1977.
    • (1991) J Bacteriol , vol.173 , pp. 1971-1977
    • Marwan, W.1    Alam, M.2    Oesterhelt, D.3
  • 76
    • 0036405357 scopus 로고    scopus 로고
    • Type IV pili and twitching motility
    • Mattick JS: Type IV pili and twitching motility. Annu Rev Microbiol 2002;56:289-314.
    • (2002) Annu Rev Microbiol , vol.56 , pp. 289-314
    • Mattick, J.S.1
  • 77
    • 0000324271 scopus 로고
    • Common architecture of type 4 fimbriae and complexes involved in macromolecular traffic
    • Mattick JS, Alm RA: Common architecture of type 4 fimbriae and complexes involved in macromolecular traffic. Trends Microbiol 1995;3:411-413.
    • (1995) Trends Microbiol , vol.3 , pp. 411-413
    • Mattick, J.S.1    Alm, R.A.2
  • 78
    • 0034618643 scopus 로고    scopus 로고
    • Pilus retraction powers bacterial twichingmotility
    • Merz AJ, So M, Sheetz MP: Pilus retraction powers bacterial twichingmotility. Nature 2000;407:98-102.
    • (2000) Nature , vol.407 , pp. 98-102
    • Merz, A.J.1    So, M.2    Sheetz, M.P.3
  • 79
    • 1942540043 scopus 로고    scopus 로고
    • Prokaryotic glycoproteins: Unexplored but important
    • Messner P: Prokaryotic glycoproteins: unexplored but important. J Bacteriol 2004;186:2517-2519.
    • (2004) J Bacteriol , vol.186 , pp. 2517-2519
    • Messner, P.1
  • 80
    • 11144246739 scopus 로고    scopus 로고
    • Bacterial and archaeal flagella as prokaryotic motility organelles
    • Mosc
    • Metlina AL: Bacterial and archaeal flagella as prokaryotic motility organelles. Biochemistry (Mosc) 2004;69:1477-1488.
    • (2004) Biochemistry , vol.69 , pp. 1477-1488
    • Metlina, A.L.1
  • 81
    • 2642559479 scopus 로고    scopus 로고
    • Self-assembly and type III protein export of the bacterial flagellum
    • Minamino T, Namba K: Self-assembly and type III protein export of the bacterial flagellum. J Mol Microbiol Biotechnol 2004;7:5-17.
    • (2004) J Mol Microbiol Biotechnol , vol.7 , pp. 5-17
    • Minamino, T.1    Namba, K.2
  • 82
    • 0030825124 scopus 로고    scopus 로고
    • Glycoproteins in prokaryotes
    • Moens S, Vanderleyden J: Glycoproteins in prokaryotes. Arch Microbiol 1997;168:169-175.
    • (1997) Arch Microbiol , vol.168 , pp. 169-175
    • Moens, S.1    Vanderleyden, J.2
  • 83
    • 13244269794 scopus 로고    scopus 로고
    • Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease
    • Moore BC, Leigh JA: Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease. J Bacteriol 2005;187:972-979.
    • (2005) J Bacteriol , vol.187 , pp. 972-979
    • Moore, B.C.1    Leigh, J.A.2
  • 84
    • 0036122161 scopus 로고    scopus 로고
    • Functional substitution of the TibC protein of enterotoxigenic Esherichia coli strains for the autotransporter adhesion heptosyltransferase of the AIDA system
    • Moorman C, Benz I, Schmidt MA: Functional substitution of the TibC protein of enterotoxigenic Esherichia coli strains for the autotransporter adhesion heptosyltransferase of the AIDA system. Infect Immun 2002;70:2264-2270.
    • (2002) Infect Immun , vol.70 , pp. 2264-2270
    • Moorman, C.1    Benz, I.2    Schmidt, M.A.3
  • 85
    • 0034633401 scopus 로고    scopus 로고
    • 2 control on the expression of flagella in the hyperthermophilic strictly hydrogenotropic methanarchaeon Methanococcus jannaschii
    • 2 control on the expression of flagella in the hyperthermophilic strictly hydrogenotropic methanarchaeon Methanococcus jannaschii. Proc Natl Acad Sci USA 2000;97:11522-11527.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11522-11527
    • Mukhopadhyay, B.1    Johnson, E.F.2    Wolfe, R.S.3
  • 86
    • 0032800749 scopus 로고    scopus 로고
    • Sequence and transcriptional studies of five clustered flagellin genes from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1
    • Nagahisa K, Ezaki S, Fujiwara S, Imanaka T, Takagi M: Sequence and transcriptional studies of five clustered flagellin genes from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1. FEMS Microbiol Lett 1999;178:183-190.
    • (1999) FEMS Microbiol Lett , vol.178 , pp. 183-190
    • Nagahisa, K.1    Ezaki, S.2    Fujiwara, S.3    Imanaka, T.4    Takagi, M.5
  • 87
    • 2342652283 scopus 로고    scopus 로고
    • The outer membrane of the hyperthermophilic archaeaon Ignicoccus: Dynamics, ultrastructure and composition
    • Nather DJ, Rachel R: The outer membrane of the hyperthermophilic archaeaon Ignicoccus: dynamics, ultrastructure and composition. Biochem Soc Trans 2003;32:199-203.
    • (2003) Biochem Soc Trans , vol.32 , pp. 199-203
    • Nather, D.J.1    Rachel, R.2
  • 88
    • 15944393490 scopus 로고    scopus 로고
    • The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation
    • Nita-Lazar M, Wacker M, Schegg B, Amber S, Aebi M: The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology 2005;15:361-367.
    • (2005) Glycobiology , vol.15 , pp. 361-367
    • Nita-Lazar, M.1    Wacker, M.2    Schegg, B.3    Amber, S.4    Aebi, M.5
  • 90
    • 0242407439 scopus 로고    scopus 로고
    • Signal processing and flagellar motor switching during phototaxis of Halobacterium salinarum
    • Nutsch T, Marwan W, Oesterhelt D, Gillies ED: Signal processing and flagellar motor switching during phototaxis of Halobacterium salinarum. Genome Res 2003a;13:2406-2412.
    • (2003) Genome Res , vol.13 , pp. 2406-2412
    • Nutsch, T.1    Marwan, W.2    Oesterhelt, D.3    Gillies, E.D.4
  • 91
    • 0242407439 scopus 로고    scopus 로고
    • Signal processing and flagellar motor switching during phototaxis of Halobacterium salinarum
    • Nutsch T, Marwan W, Oesterhelt D, Gillies ED: Signal processing and flagellar motor switching during phototaxis of Halobacterium salinarum. Genome Res 2003b;13:2406-2412.
    • (2003) Genome Res , vol.13 , pp. 2406-2412
    • Nutsch, T.1    Marwan, W.2    Oesterhelt, D.3    Gillies, E.D.4
  • 92
    • 25844525601 scopus 로고    scopus 로고
    • A quantitative model of the switch cycle of an archaeal flagellar motor and its sensory control
    • Nutsch T, Oesterhelt D, Gillies ED, Marwan W: A quantitative model of the switch cycle of an archaeal flagellar motor and its sensory control. Biophys J 2005;89:2307-2323.
    • (2005) Biophys J , vol.89 , pp. 2307-2323
    • Nutsch, T.1    Oesterhelt, D.2    Gillies, E.D.3    Marwan, W.4
  • 94
    • 0034882854 scopus 로고    scopus 로고
    • The fla gene cluster is involved in the biogenesis of flagella of Halobacterium salinarum
    • Patenge N, Berendes A, Englehardt H, Schuster SC, Oesterhelt D: The fla gene cluster is involved in the biogenesis of flagella of Halobacterium salinarum. Mol Microbiol 2001;41:653-663.
    • (2001) Mol Microbiol , vol.41 , pp. 653-663
    • Patenge, N.1    Berendes, A.2    Englehardt, H.3    Schuster, S.C.4    Oesterhelt, D.5
  • 96
    • 0032563102 scopus 로고    scopus 로고
    • Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa
    • Pepe JC, Lory S: Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa. J Biol Chem 1998;273:19120-19129.
    • (1998) J Biol Chem , vol.273 , pp. 19120-19129
    • Pepe, J.C.1    Lory, S.2
  • 97
    • 0032143972 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase from haloalkaliphilic archaeon Natronobacterium magadii
    • Polosina YY, Jarrell KF, Fedorov OV, Kostyukova AS: Nucleoside diphosphate kinase from haloalkaliphilic archaeon Natronobacterium magadii. Extremophiles 1998;2:333-338.
    • (1998) Extremophiles , vol.2 , pp. 333-338
    • Polosina, Y.Y.1    Jarrell, K.F.2    Fedorov, O.V.3    Kostyukova, A.S.4
  • 98
    • 0037469276 scopus 로고    scopus 로고
    • The genetics of glycosylation in Gram-negative bacteria
    • Power MP, Jennings MP: The genetics of glycosylation in Gram-negative bacteria. FEMS Microbiol Lett 2003;218:211-222.
    • (2003) FEMS Microbiol Lett , vol.218 , pp. 211-222
    • Power, M.P.1    Jennings, M.P.2
  • 100
    • 0037129835 scopus 로고    scopus 로고
    • Two immunologically distinct types of protofilaments can be identified in Natrialba magadii flagella
    • Pyatibratov MG, Leonard K, Tarasov VY, Fedorov OV: Two immunologically distinct types of protofilaments can be identified in Natrialba magadii flagella. FEMS Microbiol Lett 2002;212:23-27.
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 23-27
    • Pyatibratov, M.G.1    Leonard, K.2    Tarasov, V.Y.3    Fedorov, O.V.4
  • 101
    • 0342624740 scopus 로고    scopus 로고
    • Deletion alaysis of the che operon in the archaeon Halobacterium salinarium
    • Rudolph J, Oesterhelt D: Deletion alaysis of the che operon in the archaeon Halobacterium salinarium. J Mol Biol 1996;258:548-554.
    • (1996) J Mol Biol , vol.258 , pp. 548-554
    • Rudolph, J.1    Oesterhelt, D.2
  • 102
    • 0035029580 scopus 로고    scopus 로고
    • Biology of type II secretion
    • Sandkvist M: Biology of type II secretion. Mol Microbiol 2001;40:271-283.
    • (2001) Mol Microbiol , vol.40 , pp. 271-283
    • Sandkvist, M.1
  • 103
    • 0037560879 scopus 로고    scopus 로고
    • Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori
    • Schirm M, Soo EC, Aubry AJ, Austin J, Thibault P, Logan SM: Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori. Mol Microbiol 2003;48:1579-1592.
    • (2003) Mol Microbiol , vol.48 , pp. 1579-1592
    • Schirm, M.1    Soo, E.C.2    Aubry, A.J.3    Austin, J.4    Thibault, P.5    Logan, S.M.6
  • 104
    • 1942540030 scopus 로고    scopus 로고
    • Structural and genetic characterization of glycosylation of type a flagellin in Pseudomonas aeruginosa
    • Schirm M, Arora S K, Verma A, Vinogradov E, Thibault P, Ramphal R, Logan SM: Structural and genetic characterization of glycosylation of type a flagellin in Pseudomonas aeruginosa. J Bacteriol 2004;186:2523-2531.
    • (2004) J Bacteriol , vol.186 , pp. 2523-2531
    • Schirm, M.1    Arora, S.K.2    Verma, A.3    Vinogradov, E.4    Thibault, P.5    Ramphal, R.6    Logan, S.M.7
  • 105
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: Glycoproteins in bacterial pathogens
    • Schmidt MA, Riley LW, Benz I: Sweet new world: glycoproteins in bacterial pathogens. Trends Microbiol 2003;11:554-561.
    • (2003) Trends Microbiol , vol.11 , pp. 554-561
    • Schmidt, M.A.1    Riley, L.W.2    Benz, I.3
  • 107
    • 27844477243 scopus 로고    scopus 로고
    • Isolation and characterization of methylotrophic methanogens from anoxic marine sediments in Skan Bay, Alaska: Description of Methanococcoides alaskense sp. nov., and emended description of Methanosarcina baltica
    • Singh N, Kendall MM, Liu Y, Boone DR: Isolation and characterization of methylotrophic methanogens from anoxic marine sediments in Skan Bay, Alaska: description of Methanococcoides alaskense sp. nov., and emended description of Methanosarcina baltica. Int J Syst Evol Microbiol 2005;55:2531-2538.
    • (2005) Int J Syst Evol Microbiol , vol.55 , pp. 2531-2538
    • Singh, N.1    Kendall, M.M.2    Liu, Y.3    Boone, D.R.4
  • 108
    • 0035810950 scopus 로고    scopus 로고
    • Direct observation of extension and retraction of type IV pili
    • Skerker JM, Berg HC: Direct observation of extension and retraction of type IV pili. Proc Natl Acad Sci USA 2001;98:6901-6904.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6901-6904
    • Skerker, J.M.1    Berg, H.C.2
  • 109
    • 0018195592 scopus 로고
    • Regular arrays of macromolecules on bacterial cell walls: Structure, chemistry, assembly, and function
    • Sleytr UB: Regular arrays of macromolecules on bacterial cell walls: structure, chemistry, assembly, and function. Int Rev Cytol 1978;53:1-62.
    • (1978) Int Rev Cytol , vol.53 , pp. 1-62
    • Sleytr, U.B.1
  • 110
    • 0004360090 scopus 로고    scopus 로고
    • Disk-like lamellar structure as part of the archaeal flagellar apparatus
    • Speranskii VV, Metlina AL, Novikova TM, Bakeyeva LY: Disk-like lamellar structure as part of the archaeal flagellar apparatus. Biophysics 1996;41:167-173.
    • (1996) Biophysics , vol.41 , pp. 167-173
    • Speranskii, V.V.1    Metlina, A.L.2    Novikova, T.M.3    Bakeyeva, L.Y.4
  • 111
    • 0029879021 scopus 로고    scopus 로고
    • A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for the biogenesis of a type IV pilus
    • Stone KD, Zhang HZ, Carlson LK, Donnenberg MS: A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for the biogenesis of a type IV pilus. Mol Microbiol 1996;20:325-337.
    • (1996) Mol Microbiol , vol.20 , pp. 325-337
    • Stone, K.D.1    Zhang, H.Z.2    Carlson, L.K.3    Donnenberg, M.S.4
  • 112
    • 0027385590 scopus 로고
    • Structure-function and biogenesis of the type IV pili
    • Strom MS, Lory S: Structure-function and biogenesis of the type IV pili. Annu Rev Genet 1993;47:565-596.
    • (1993) Annu Rev Genet , vol.47 , pp. 565-596
    • Strom, M.S.1    Lory, S.2
  • 113
    • 0023235232 scopus 로고
    • Halobacterial glycoprotein biosynthesis
    • Sumper M: Halobacterial glycoprotein biosynthesis. Biochim Biophys Acta 1987;906:69-79.
    • (1987) Biochim Biophys Acta , vol.906 , pp. 69-79
    • Sumper, M.1
  • 114
    • 77956818765 scopus 로고
    • Bacterial glycoproteins
    • Montreuil J, Schachter H, Vliegenthart JFG (eds): New York, Elsevier Science
    • Sumper M, Wieland FT: Bacterial glycoproteins; in Montreuil J, Schachter H, Vliegenthart JFG (eds): Glycoproteins. New York, Elsevier Science, 1995, pp 455-473.
    • (1995) Glycoproteins , pp. 455-473
    • Sumper, M.1    Wieland, F.T.2
  • 115
    • 2942584862 scopus 로고    scopus 로고
    • Diversity of chemotaxis machanisms among the Bacteria and Archaea
    • Szurmant H, Ordal GW: Diversity of chemotaxis machanisms among the Bacteria and Archaea. Microbiol Mol Biol Rev 2004;68:301-319.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 301-319
    • Szurmant, H.1    Ordal, G.W.2
  • 117
    • 0030590217 scopus 로고    scopus 로고
    • Motility protein complexes in the bacterial flagellar motor
    • Tang H, Braun TF, Blair DF: Motility protein complexes in the bacterial flagellar motor. J Mol Biol 1996;261:209-221.
    • (1996) J Mol Biol , vol.261 , pp. 209-221
    • Tang, H.1    Braun, T.F.2    Blair, D.F.3
  • 118
    • 0035860764 scopus 로고    scopus 로고
    • Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin
    • Thibault P, Logan SM, Kelly JF, Brisson JR, Ewing CP, Trust TJ, Guerry P: Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. J Biol Chem 2001;276:34862-34870.
    • (2001) J Biol Chem , vol.276 , pp. 34862-34870
    • Thibault, P.1    Logan, S.M.2    Kelly, J.F.3    Brisson, J.R.4    Ewing, C.P.5    Trust, T.J.6    Guerry, P.7
  • 119
    • 0035213102 scopus 로고    scopus 로고
    • Characterization of flagellum gene families of methanogenic archaea and localization of novel flagellum accessory proteins
    • Thomas NA, Jarrell KF: Characterization of flagellum gene families of methanogenic archaea and localization of novel flagellum accessory proteins. J Bacteriol 2001;183:7154-7164.
    • (2001) J Bacteriol , vol.183 , pp. 7154-7164
    • Thomas, N.A.1    Jarrell, K.F.2
  • 120
    • 0035105745 scopus 로고    scopus 로고
    • The archaeal flagellum: A different kind of prokaryotic motility structure
    • Thomas NA, Bardy SL, Jarrell KF: The archaeal flagellum: a different kind of prokaryotic motility structure. FEMS Microbiol Rev 2001a;25:147-174.
    • (2001) FEMS Microbiol Rev , vol.25 , pp. 147-174
    • Thomas, N.A.1    Bardy, S.L.2    Jarrell, K.F.3
  • 121
    • 0035028932 scopus 로고    scopus 로고
    • Identification of amino acids in the leader peptide of Methanococcus voltae preflagellin that are important in posttranslational processing
    • Thomas NA, Chao ED, Jarrell KF: Identification of amino acids in the leader peptide of Methanococcus voltae preflagellin that are important in posttranslational processing. Arch Microbiol 2001b;175:263-269.
    • (2001) Arch Microbiol , vol.175 , pp. 263-269
    • Thomas, N.A.1    Chao, E.D.2    Jarrell, K.F.3
  • 122
    • 0036436988 scopus 로고    scopus 로고
    • Mutants in flaI and flaI of the archaeon Methanococcus voltae are deficient in flagellum assembly
    • Thomas NA, Mueller S, Klein A, Jarrell KF: Mutants in flaI and flaI of the archaeon Methanococcus voltae are deficient in flagellum assembly. Mol Microbiol 2002;46:879-887.
    • (2002) Mol Microbiol , vol.46 , pp. 879-887
    • Thomas, N.A.1    Mueller, S.2    Klein, A.3    Jarrell, K.F.4
  • 123
    • 0029849368 scopus 로고    scopus 로고
    • Cloning and characterization of bfpTVW, genes required for the transcription of bfpA in enteropathogenic Escherichia coli
    • Tobe T, Schoolnik GK, Sohel I, Bustamante VH, Puente JL: Cloning and characterization of bfpTVW, genes required for the transcription of bfpA in enteropathogenic Escherichia coli. Mol Microbiol 1996;21:963-975.
    • (1996) Mol Microbiol , vol.21 , pp. 963-975
    • Tobe, T.1    Schoolnik, G.K.2    Sohel, I.3    Bustamante, V.H.4    Puente, J.L.5
  • 124
    • 13844271970 scopus 로고    scopus 로고
    • Refining the structure of the Halobacterium salinarum flagellar filament using the iterative helical real space reconstruction method: Insights into polymorphism
    • Trachtenberg S, Galkin VE, Egalman EH: Refining the structure of the Halobacterium salinarum flagellar filament using the iterative helical real space reconstruction method: insights into polymorphism. J Mol Biol 2005;346:665-676.
    • (2005) J Mol Biol , vol.346 , pp. 665-676
    • Trachtenberg, S.1    Galkin, V.E.2    Egalman, E.H.3
  • 125
    • 0037387036 scopus 로고    scopus 로고
    • Bacterial glycoproteins: Functions, biosynthesis and applications
    • Upreti RK, Kumar M, Shankar V: Bacterial glycoproteins: functions, biosynthesis and applications. Proteomics 2003;3:363-379.
    • (2003) Proteomics , vol.3 , pp. 363-379
    • Upreti, R.K.1    Kumar, M.2    Shankar, V.3
  • 127
    • 0037853309 scopus 로고    scopus 로고
    • Type IV pili formed by the type II secreton: Specificity, composition, bundling, polar localization, and surface presentation of peptides
    • Vignon G, Köhler R, Larquet E, Giroux S, Prévost M, Roux P, Pugsley A: Type IV pili formed by the type II secreton: specificity, composition, bundling, polar localization, and surface presentation of peptides. J Bacteriol 2003;185:3416-3428.
    • (2003) J Bacteriol , vol.185 , pp. 3416-3428
    • Vignon, G.1    Köhler, R.2    Larquet, E.3    Giroux, S.4    Prévost, M.5    Roux, P.6    Pugsley, A.7
  • 128
    • 20444488776 scopus 로고    scopus 로고
    • Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae
    • Voisin S, Houliston RS, Kelly J, Brisson J-R, Watson D, Bardy SL, Jarrell KF, Logan SM: Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae. J Biol Chem 2005;17:16586-16593.
    • (2005) J Biol Chem , vol.17 , pp. 16586-16593
    • Voisin, S.1    Houliston, R.S.2    Kelly, J.3    Brisson, J.-R.4    Watson, D.5    Bardy, S.L.6    Jarrell, K.F.7    Logan, S.M.8
  • 130
    • 0034851055 scopus 로고    scopus 로고
    • Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics
    • Vosseller K, Wells L, Hart GW: Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics. Biochimie 2001;83:575-581.
    • (2001) Biochimie , vol.83 , pp. 575-581
    • Vosseller, K.1    Wells, L.2    Hart, G.W.3
  • 131
    • 0032742727 scopus 로고    scopus 로고
    • Motility in Myxoococcus xanthus and its role in developmental aggregation
    • Ward MJ, Zusman DR: Motility in Myxoococcus xanthus and its role in developmental aggregation. Curr Opin Microbiol 1999;2:624-629.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 624-629
    • Ward, M.J.1    Zusman, D.R.2
  • 133
    • 0025878130 scopus 로고
    • Characterization of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialised protein export system widespread in eubacteria
    • Whitchurch CB, Hobbs M, Livingston SP, Krishnapillai V, Mattick JS: Characterization of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialised protein export system widespread in eubacteria. Gene 1990;101:33-44.
    • (1990) Gene , vol.101 , pp. 33-44
    • Whitchurch, C.B.1    Hobbs, M.2    Livingston, S.P.3    Krishnapillai, V.4    Mattick, J.S.5
  • 135
    • 0027200487 scopus 로고
    • Bacterial flagellar filaments and their component flagellins
    • Wilson DR, Beveridge TJ: Bacterial flagellar filaments and their component flagellins. Can J Microbiol 1993;39:451-472.
    • (1993) Can J Microbiol , vol.39 , pp. 451-472
    • Wilson, D.R.1    Beveridge, T.J.2
  • 136
    • 0036220599 scopus 로고    scopus 로고
    • Transcriptional, chemosensory and cell-contact-dependent regulation of type IV pilus expression
    • Winther-Larsen HC, Koomey M: Transcriptional, chemosensory and cell-contact-dependent regulation of type IV pilus expression. Curr Opin Microbiol 2002;5:173-178.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 173-178
    • Winther-Larsen, H.C.1    Koomey, M.2
  • 137
    • 0034406525 scopus 로고    scopus 로고
    • Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili
    • Wolfgang M, van Putten JPM, Hayes SF, Dorward D, Kooney M: Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili. EMBO J 2000;19:6408-6418.
    • (2000) EMBO J , vol.19 , pp. 6408-6418
    • Wolfgang, M.1    Van Putten, J.P.M.2    Hayes, S.F.3    Dorward, D.4    Kooney, M.5
  • 138
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K, Maki-Yonekura S, Namba K: Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 2003;424:643-650.
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 139
    • 0032416590 scopus 로고    scopus 로고
    • Exchange of Ser-4 for Val, Leu or Asn in the sequon Asn-Ala-Ser does not prevent N-glycosylation of the cell surface glycoprotein from Halobacterium halobium
    • Zeitler R, Hochmuth E, Deutzmann R, Sumper M: Exchange of Ser-4 for Val, Leu or Asn in the sequon Asn-Ala-Ser does not prevent N-glycosylation of the cell surface glycoprotein from Halobacterium halobium. Glycobiology 1998;8:1157-1164.
    • (1998) Glycobiology , vol.8 , pp. 1157-1164
    • Zeitler, R.1    Hochmuth, E.2    Deutzmann, R.3    Sumper, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.