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Volumn 14, Issue 3, 2011, Pages 357-363

Archaeal type IV pilus-like structures-evolutionarily conserved prokaryotic surface organelles

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEBACTERIUM; BACTERIAL CELL; BACTERIAL GENETICS; BACTERIAL GENOME; BACTERIUM PILUS; BIOSYNTHESIS; CELL ORGANELLE; COMPUTER MODEL; GENE SEQUENCE; MOLECULAR EVOLUTION; NONHUMAN; REVIEW;

EID: 79958816876     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2011.03.002     Document Type: Review
Times cited : (70)

References (47)
  • 1
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • Craig L., Pique M.E., Tainer J.A. 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
  • 2
    • 67349199521 scopus 로고    scopus 로고
    • Diversity of archaeal type IV pilin-like structures
    • Albers S.V., Pohlschroder M. Diversity of archaeal type IV pilin-like structures. Extremophiles 2009, 13:403-410.
    • (2009) Extremophiles , vol.13 , pp. 403-410
    • Albers, S.V.1    Pohlschroder, M.2
  • 4
    • 78149443620 scopus 로고    scopus 로고
    • Bacterial contact-dependent delivery systems
    • Hayes C.S., Aoki S.K., Low D.A. Bacterial contact-dependent delivery systems. Annu Rev Genet 2010, 44:71-90.
    • (2010) Annu Rev Genet , vol.44 , pp. 71-90
    • Hayes, C.S.1    Aoki, S.K.2    Low, D.A.3
  • 5
    • 51049118119 scopus 로고    scopus 로고
    • Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria
    • Fronzes R., Remaut H., Waksman G. Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria. EMBO J 2008, 27:2271-2280.
    • (2008) EMBO J , vol.27 , pp. 2271-2280
    • Fronzes, R.1    Remaut, H.2    Waksman, G.3
  • 7
    • 0037288048 scopus 로고    scopus 로고
    • Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography
    • Nickell S., Hegerl R., Baumeister W., Rachel R. Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography. J Struct Biol 2003, 141:34-42.
    • (2003) J Struct Biol , vol.141 , pp. 34-42
    • Nickell, S.1    Hegerl, R.2    Baumeister, W.3    Rachel, R.4
  • 8
    • 17144417351 scopus 로고    scopus 로고
    • The unique structure of archaeal 'hami', highly complex cell appendages with nano-grappling hooks
    • Moissl C., Rachel R., Briegel A., Engelhardt H., Huber R. The unique structure of archaeal 'hami', highly complex cell appendages with nano-grappling hooks. Mol Microbiol 2005, 56:361-370.
    • (2005) Mol Microbiol , vol.56 , pp. 361-370
    • Moissl, C.1    Rachel, R.2    Briegel, A.3    Engelhardt, H.4    Huber, R.5
  • 9
    • 33846567505 scopus 로고    scopus 로고
    • Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases
    • Szabo Z., Stahl A.O., Albers S.V., Kissinger J.C., Driessen A.J., Pohlschroder M. Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases. J Bacteriol 2007, 189:772-778.
    • (2007) J Bacteriol , vol.189 , pp. 772-778
    • Szabo, Z.1    Stahl, A.O.2    Albers, S.V.3    Kissinger, J.C.4    Driessen, A.J.5    Pohlschroder, M.6
  • 10
    • 33748768732 scopus 로고    scopus 로고
    • The archaeabacterial flagellar filament: a bacterial propeller with a pilus-like structure
    • Trachtenberg S., Cohen-Krausz S. The archaeabacterial flagellar filament: a bacterial propeller with a pilus-like structure. J Mol Microbiol Biotechnol 2006, 11:208-220.
    • (2006) J Mol Microbiol Biotechnol , vol.11 , pp. 208-220
    • Trachtenberg, S.1    Cohen-Krausz, S.2
  • 11
    • 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 V.E., Egelman E.H. 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    Egelman, E.H.3
  • 13
    • 33748757929 scopus 로고    scopus 로고
    • Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications
    • Ng S.Y., Chaban B., Jarrell K.F. Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications. J Mol Microbiol Biotechnol 2006, 11:167-191.
    • (2006) J Mol Microbiol Biotechnol , vol.11 , pp. 167-191
    • Ng, S.Y.1    Chaban, B.2    Jarrell, K.F.3
  • 14
    • 33947360771 scopus 로고    scopus 로고
    • Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II secretion system via the signal recognition particle-Sec pathway
    • Arts J., van Boxtel R., Filloux A., Tommassen J., Koster M. Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II secretion system via the signal recognition particle-Sec pathway. J Bacteriol 2007, 189:2069-2076.
    • (2007) J Bacteriol , vol.189 , pp. 2069-2076
    • Arts, J.1    van Boxtel, R.2    Filloux, A.3    Tommassen, J.4    Koster, M.5
  • 15
    • 33947397246 scopus 로고    scopus 로고
    • Signal recognition particle-dependent inner membrane targeting of the PulG pseudopilin component of a type II secretion system
    • Francetic O., Buddelmeijer N., Lewenza S., Kumamoto C.A., Pugsley A.P. Signal recognition particle-dependent inner membrane targeting of the PulG pseudopilin component of a type II secretion system. J Bacteriol 2007, 189:1783-1793.
    • (2007) J Bacteriol , vol.189 , pp. 1783-1793
    • Francetic, O.1    Buddelmeijer, N.2    Lewenza, S.3    Kumamoto, C.A.4    Pugsley, A.P.5
  • 16
    • 0027528605 scopus 로고
    • A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family
    • Strom M.S., Nunn D.N., Lory S. A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family. Proc Natl Acad Sci U S A 1993, 90:2404-2408.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2404-2408
    • Strom, M.S.1    Nunn, D.N.2    Lory, S.3
  • 17
    • 77955936558 scopus 로고    scopus 로고
    • Architecture of the type II secretion and type IV pilus machineries
    • Ayers M., Howell P.L., Burrows L.L. Architecture of the type II secretion and type IV pilus machineries. Future Microbiol 2010, 5:1203-1218.
    • (2010) Future Microbiol , vol.5 , pp. 1203-1218
    • Ayers, M.1    Howell, P.L.2    Burrows, L.L.3
  • 18
    • 0037133374 scopus 로고    scopus 로고
    • FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity
    • Bardy S.L., Jarrell K.F. 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
  • 19
    • 0038170287 scopus 로고    scopus 로고
    • Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity
    • Albers S.V., Szabo Z., Driessen A.J. 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.3
  • 20
    • 0025978598 scopus 로고
    • Amino acid substitutions in pilin of Pseudomonas aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly
    • Strom M.S., Lory S. Amino acid substitutions in pilin of Pseudomonas aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly. J Biol Chem 1991, 266:1656-1664.
    • (1991) J Biol Chem , vol.266 , pp. 1656-1664
    • Strom, M.S.1    Lory, S.2
  • 22
    • 0034882854 scopus 로고    scopus 로고
    • The fla gene cluster is involved in the biogenesis of flagella in Halobacterium salinarum
    • Patenge N., Berendes A., Engelhardt H., Schuster S.C., Oesterhelt D. The fla gene cluster is involved in the biogenesis of flagella in Halobacterium salinarum. Mol Microbiol 2001, 41:653-663.
    • (2001) Mol Microbiol , vol.41 , pp. 653-663
    • Patenge, N.1    Berendes, A.2    Engelhardt, H.3    Schuster, S.C.4    Oesterhelt, D.5
  • 23
    • 35448929983 scopus 로고    scopus 로고
    • Systematic deletion analyses of the fla genes in the flagella operon identify several genes essential for proper assembly and function of flagella in the archaeon, Methanococcus maripaludis
    • Chaban B., Ng S.Y., Kanbe M., Saltzman I., Nimmo G., Aizawa S., Jarrell K.F. Systematic deletion analyses of the fla genes in the flagella operon identify several genes essential for proper assembly and function of flagella in the archaeon, Methanococcus maripaludis. Mol Microbiol 2007, 66:596-609.
    • (2007) Mol Microbiol , vol.66 , pp. 596-609
    • Chaban, B.1    Ng, S.Y.2    Kanbe, M.3    Saltzman, I.4    Nimmo, G.5    Aizawa, S.6    Jarrell, K.F.7
  • 24
    • 54249084495 scopus 로고    scopus 로고
    • Flagellar rotation in the archaeon Halobacterium salinarum depends on ATP
    • Streif S., Staudinger W.F., Marwan W., Oesterhelt D. Flagellar rotation in the archaeon Halobacterium salinarum depends on ATP. J Mol Biol 2008, 384:1-8.
    • (2008) J Mol Biol , vol.384 , pp. 1-8
    • Streif, S.1    Staudinger, W.F.2    Marwan, W.3    Oesterhelt, D.4
  • 25
    • 77953975121 scopus 로고    scopus 로고
    • Haloferax volcanii flagella are required for motility but are not involved in PibD-dependent surface adhesion
    • Tripepi M., Imam S., Pohlschroder M. Haloferax volcanii flagella are required for motility but are not involved in PibD-dependent surface adhesion. J Bacteriol 2010, 192:3093-3102.
    • (2010) J Bacteriol , vol.192 , pp. 3093-3102
    • Tripepi, M.1    Imam, S.2    Pohlschroder, M.3
  • 26
    • 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 S.M., Jarrell K.F. 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
  • 27
    • 48149087089 scopus 로고    scopus 로고
    • Identification of a putative acetyltransferase gene, MMP0350, which affects proper assembly of both flagella and pili in the archaeon Methanococcus maripaludis
    • VanDyke D.J., Wu J., Ng S.Y., Kanbe M., Chaban B., Aizawa S., Jarrell K.F. Identification of a putative acetyltransferase gene, MMP0350, which affects proper assembly of both flagella and pili in the archaeon Methanococcus maripaludis. J Bacteriol 2008, 190:5300-5307.
    • (2008) J Bacteriol , vol.190 , pp. 5300-5307
    • VanDyke, D.J.1    Wu, J.2    Ng, S.Y.3    Kanbe, M.4    Chaban, B.5    Aizawa, S.6    Jarrell, K.F.7
  • 28
    • 40949158969 scopus 로고    scopus 로고
    • Multicomponent nature of Halobacterium salinarum flagella
    • Beznosov S.N., Piatibratov M.G., Fedorov O.V. Multicomponent nature of Halobacterium salinarum flagella. Mikrobiologiia 2007, 76:494-501.
    • (2007) Mikrobiologiia , vol.76 , pp. 494-501
    • Beznosov, S.N.1    Piatibratov, M.G.2    Fedorov, O.V.3
  • 29
    • 0029881205 scopus 로고    scopus 로고
    • Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae
    • Jarrell K.F., Bayley D.P., 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
  • 32
    • 12444272635 scopus 로고    scopus 로고
    • Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin
    • Craig L., Taylor R.K., Pique M.E., Adair B.D., Arvai A.S., Singh M., Lloyd S.J., Shin D.S., Getzoff E.D., Yeager M., et al. Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin. Mol Cell 2003, 11:1139-1150.
    • (2003) Mol Cell , vol.11 , pp. 1139-1150
    • Craig, L.1    Taylor, R.K.2    Pique, M.E.3    Adair, B.D.4    Arvai, A.S.5    Singh, M.6    Lloyd, S.J.7    Shin, D.S.8    Getzoff, E.D.9    Yeager, M.10
  • 34
    • 33749345268 scopus 로고    scopus 로고
    • Flagella of Pyrococcus furiosus: multifunctional organelles, made for swimming, adhesion to various surfaces, and cell-cell contacts
    • Nather D.J., Rachel R., Wanner G., Wirth R. Flagella of Pyrococcus furiosus: multifunctional organelles, made for swimming, adhesion to various surfaces, and cell-cell contacts. J Bacteriol 2006, 188:6915-6923.
    • (2006) J Bacteriol , vol.188 , pp. 6915-6923
    • Nather, D.J.1    Rachel, R.2    Wanner, G.3    Wirth, R.4
  • 37
    • 0024447751 scopus 로고
    • The mechanism of DNA transfer in the mating system of an archaebacterium
    • Rosenshine I., Tchelet R., Mevarech M. The mechanism of DNA transfer in the mating system of an archaebacterium. Science 1989, 245:1387-1389.
    • (1989) Science , vol.245 , pp. 1387-1389
    • Rosenshine, I.1    Tchelet, R.2    Mevarech, M.3
  • 38
    • 0032808951 scopus 로고    scopus 로고
    • Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein
    • Albers S.V., Elferink M.G., Charlebois R.L., Sensen C.W., Driessen A.J.M., Konings W.N. Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein. J Bacteriol 1999, 181:4285-4291.
    • (1999) J Bacteriol , vol.181 , pp. 4285-4291
    • Albers, S.V.1    Elferink, M.G.2    Charlebois, R.L.3    Sensen, C.W.4    Driessen, A.J.M.5    Konings, W.N.6
  • 39
    • 0032984481 scopus 로고    scopus 로고
    • A unique short signal sequence in membrane anchored proteins of Archaea
    • Albers S.V., Konings W.N., Driessen A.J.M. A unique short signal sequence in membrane anchored proteins of Archaea. Mol Microbiol 1999, 31:1595-1596.
    • (1999) Mol Microbiol , vol.31 , pp. 1595-1596
    • Albers, S.V.1    Konings, W.N.2    Driessen, A.J.M.3
  • 40
    • 34247515309 scopus 로고    scopus 로고
    • Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus
    • Zolghadr B., Weber S., Szabo Z., Driessen A.J.M., Albers S.V. Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus. Mol Microbiol 2007, 64:795-806.
    • (2007) Mol Microbiol , vol.64 , pp. 795-806
    • Zolghadr, B.1    Weber, S.2    Szabo, Z.3    Driessen, A.J.M.4    Albers, S.V.5
  • 41
    • 0242360953 scopus 로고    scopus 로고
    • DNA transport during transformation
    • Chen I., Dubnau D. DNA transport during transformation. Front Biosci 2003, 8:S544-S556.
    • (2003) Front Biosci , vol.8
    • Chen, I.1    Dubnau, D.2
  • 42
    • 0024429977 scopus 로고
    • Nucleotide sequence and genetic organization of the Bacillus subtilis comG operon
    • Albano M., Breitling R., Dubnau D.A. Nucleotide sequence and genetic organization of the Bacillus subtilis comG operon. J Bacteriol 1989, 171:5386-5404.
    • (1989) J Bacteriol , vol.171 , pp. 5386-5404
    • Albano, M.1    Breitling, R.2    Dubnau, D.A.3
  • 43
    • 0033958226 scopus 로고    scopus 로고
    • Posttranslational processing of Methanococcus voltae preflagellin by preflagellin peptidases of M. voltae
    • Correia J.D., Jarrell K.F. Posttranslational processing of Methanococcus voltae preflagellin by preflagellin peptidases of M. voltae. J Bacteriol 2000, 182:855-858.
    • (2000) J Bacteriol , vol.182 , pp. 855-858
    • Correia, J.D.1    Jarrell, K.F.2
  • 44
    • 0025944413 scopus 로고
    • Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria
    • Kaufman M.R., Seyer J.M., Taylor R.K. Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria. Genes Dev 1991, 5:1834-1846.
    • (1991) Genes Dev , vol.5 , pp. 1834-1846
    • Kaufman, M.R.1    Seyer, J.M.2    Taylor, R.K.3
  • 45
    • 0027337742 scopus 로고
    • Processing and methylation of PuIG, a pilin-like component of the general secretory pathway of Klebsiella oxytoca
    • Pugsley A.P. Processing and methylation of PuIG, a pilin-like component of the general secretory pathway of Klebsiella oxytoca. Mol Microbiol 1993, 9:295-308.
    • (1993) Mol Microbiol , vol.9 , pp. 295-308
    • Pugsley, A.P.1
  • 46
    • 0031950535 scopus 로고    scopus 로고
    • Cell surface localization and processing of the ComG proteins, required for DNA binding during transformation of Bacillus subtilis
    • Chung Y.S., Breidt F., Dubnau D. Cell surface localization and processing of the ComG proteins, required for DNA binding during transformation of Bacillus subtilis. Mol Microbiol 1998, 29:905-913.
    • (1998) Mol Microbiol , vol.29 , pp. 905-913
    • Chung, Y.S.1    Breidt, F.2    Dubnau, D.3
  • 47
    • 79959304731 scopus 로고    scopus 로고
    • Model organisms for genetics in the domain Archaea: methanogens, halophiles, Thermococcales and Sulfolobales.
    • Leigh JA, Albers SV, Atomi H, Allers T: Model organisms for genetics in the domain Archaea: methanogens, halophiles, Thermococcales and Sulfolobales. FEMS Rev. in press.
    • FEMS Rev. in press.
    • Leigh, J.A.1    Albers, S.V.2    Atomi, H.3    Allers, T.4


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