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Volumn 3, Issue 1, 2013, Pages 86-117

Surface appendages of archaea: Structure, function, genetics and assembly

Author keywords

Archaeal flagella; Archaella; Bindosome; Cannulae; Glycosylation; Hami; Type IV pili

Indexed keywords


EID: 84893528584     PISSN: None     EISSN: 20751729     Source Type: Journal    
DOI: 10.3390/life3010086     Document Type: Review
Times cited : (45)

References (128)
  • 2
    • 78650295170 scopus 로고    scopus 로고
    • Archaea-timeline of the third domain
    • Cavicchioli, R. Archaea-timeline of the third domain. Nat. Rev. Microbiol. 2011, 9, 51-61.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 51-61
    • Cavicchioli, R.1
  • 5
    • 79958816876 scopus 로고    scopus 로고
    • Archaeal type IV pilus-like structures-evolutionarily conserved prokaryotic surface organelles
    • Pohlschroder, M.; Ghosh, A.; Tripepi, M.; Albers, S.V. Archaeal type IV pilus-like structures-evolutionarily conserved prokaryotic surface organelles. Curr. Opin. Microbiol. 2011, 14, 1-7.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 1-7
    • Pohlschroder, M.1    Ghosh, A.2    Tripepi, M.3    Albers, S.V.4
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0028842805 scopus 로고
    • Ultrastructure of the hyperthermophilic archaeon Pyrodictium. abyssi
    • Rieger, G.; Rachel, R.; Hermann, R.; Stetter, K.O. Ultrastructure of the hyperthermophilic archaeon Pyrodictium. abyssi. J. Struct. Biol. 1995, 115, 78-87.
    • (1995) J. Struct. Biol. , vol.115 , pp. 78-87
    • Rieger, G.1    Rachel, R.2    Hermann, R.3    Stetter, K.O.4
  • 9
    • 84870554600 scopus 로고    scopus 로고
    • Structure and function of the adhesive type IV pilus of Sulfolobus. acidocaldarius
    • Henche, A.L.; Ghosh, A.; Yu, X.; Jeske, T.; Egelman, E.; Albers, S.V. Structure and function of the adhesive type IV pilus of Sulfolobus. acidocaldarius. Environ. Microbiol. 2012, 14, 3188-3202.
    • (2012) Environ. Microbiol. , vol.14 , pp. 3188-3202
    • Henche, A.L.1    Ghosh, A.2    Yu, X.3    Jeske, T.4    Egelman, E.5    Albers, S.V.6
  • 10
    • 84864853841 scopus 로고    scopus 로고
    • Filaments from Ignicoccus hospitalis show diversity of packing in proteins containing N-terminal type IV pilin helices
    • Yu, X.; Goforth, C.; Meyer, C.; Rachel, R.; Schröder, G.F.; Egelman, E.H. Filaments from Ignicoccus hospitalis show diversity of packing in proteins containing N-terminal type IV pilin helices. J. Mol. Biol. 2012, 422, 274-281.
    • (2012) J. Mol. Biol. , vol.422 , pp. 274-281
    • Yu, X.1    Goforth, C.2    Meyer, C.3    Rachel, R.4    Schröder, G.F.5    Egelman, E.H.6
  • 12
    • 84862754646 scopus 로고    scopus 로고
    • The archaellum: An old motility structure with a new name
    • Jarrell, K.F.; Albers, S.V. The archaellum: an old motility structure with a new name. Trends Microbiol. 2012, 20, 307-312.
    • (2012) Trends Microbiol. , vol.20 , pp. 307-312
    • Jarrell, K.F.1    Albers, S.V.2
  • 14
    • 43849084346 scopus 로고    scopus 로고
    • The surprisingly diverse ways that prokaryotes move
    • Jarrell, K.F.; McBride, M.J. The surprisingly diverse ways that prokaryotes move. Nat. Rev. Microbiol. 2008, 6, 466-476.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 466-476
    • Jarrell, K.F.1    McBride, M.J.2
  • 15
    • 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
  • 16
    • 79551473399 scopus 로고    scopus 로고
    • Assembly and function of the archaeal flagellum
    • Ghosh, A.; Albers, S.V. Assembly and function of the archaeal flagellum. Biochem. Soc. Trans. 2011, 39, 64-69.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 64-69
    • Ghosh, A.1    Albers, S.V.2
  • 18
    • 84867900955 scopus 로고    scopus 로고
    • Response to Jarrell and Albers: The name says it all
    • Eichler, J. Response to Jarrell and Albers: the name says it all. Trends Microbiol. 2012, 20, 512-513.
    • (2012) Trends Microbiol. , vol.20 , pp. 512-513
    • Eichler, J.1
  • 19
    • 84867900351 scopus 로고    scopus 로고
    • Response to Jarrell and Albers: Seven letters less does not say more
    • Wirth, R. Response to Jarrell and Albers: seven letters less does not say more. Trends Microbiol. 2012, 20, 511-512.
    • (2012) Trends Microbiol. , vol.20 , pp. 511-512
    • Wirth, R.1
  • 20
    • 79958073627 scopus 로고    scopus 로고
    • Model organisms for genetics in the domain archaea: Methanogens, halophiles, Thermococcales and Sulfolobales
    • Leigh, J.A.; Albers, S.V.; Atomi, H.; Allers, T. Model organisms for genetics in the domain archaea: methanogens, halophiles, Thermococcales and Sulfolobales. FEMS Microbiol. Rev. 2011, 35, 577-608.
    • (2011) FEMS Microbiol. Rev. , vol.35 , pp. 577-608
    • Leigh, J.A.1    Albers, S.V.2    Atomi, H.3    Allers, T.4
  • 21
    • 37449032773 scopus 로고    scopus 로고
    • The flagellar filament structure of the extreme acidothermophile Sulfolobus. shibatae B12 suggests that archaeabacterial flagella have a unique and common symmetry and design
    • Cohen-Krausz, S.; Trachtenberg, S. The flagellar filament structure of the extreme acidothermophile Sulfolobus. shibatae B12 suggests that archaeabacterial flagella have a unique and common symmetry and design. J. Mol. Biol. 2008, 375, 1113-1124.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1113-1124
    • Cohen-Krausz, S.1    Trachtenberg, S.2
  • 22
    • 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
  • 23
    • 0345257806 scopus 로고    scopus 로고
    • Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus. voltae
    • Bardy, S.L.; Jarrell, K.F. 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
  • 24
    • 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.M.; 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.M.5    Pohlschroder, M.6
  • 25
    • 0038170287 scopus 로고    scopus 로고
    • M. Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity
    • Albers, S.V.; Szabo, Z.; Driessen, A.J. M. 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
  • 26
    • 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
  • 27
    • 77956846877 scopus 로고    scopus 로고
    • S-layer glycoproteins and flagellins: Reporters of archaeal posttranslational modifications
    • doi:10.1155/2010/612948
    • Jarrell, K.F.; Jones, G.M.; Kandiba, L.; Nair, D.B.; Eichler, J. S-layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications. Archaea. 2010, doi:10.1155/2010/612948.
    • (2010) Archaea
    • Jarrell, K.F.1    Jones, G.M.2    Kandiba, L.3    Nair, D.B.4    Eichler, J.5
  • 30
    • 84866392761 scopus 로고    scopus 로고
    • N-glycosylation of Haloferax. volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella
    • Tripepi, M.; You, J.; Temel, S.; Önder, Ö.; Brisson, D.; Pohlschröder, M. N-glycosylation of Haloferax. volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella. J. Bacteriol. 2012, 194, 4876-4887.
    • (2012) J. Bacteriol. , vol.194 , pp. 4876-4887
    • Tripepi, M.1    You, J.2    Temel, S.3    Önder, O.4    Brisson, D.5    Pohlschröder, M.6
  • 31
    • 79955002680 scopus 로고    scopus 로고
    • Flagella and pili are both necessary for efficient attachment of Methanococcus. maripaludis to surfaces
    • Jarrell, K.F.; Stark, M.; Nair, D.B.; Chong, J.P.J. Flagella and pili are both necessary for efficient attachment of Methanococcus. maripaludis to surfaces. FEMS Microbiol. Lett. 2011, 319, 44-50.
    • (2011) FEMS Microbiol. Lett. , vol.319 , pp. 44-50
    • Jarrell, K.F.1    Stark, M.2    Nair, D.B.3    Chong, J.P.J.4
  • 32
    • 84155172916 scopus 로고    scopus 로고
    • Influence of cell surface structures on crenarchaeal biofilm formation using a thermostable green fluorescent protein
    • Henche, A.L.; Koerdt, A.; Ghosh, A.; Albers, S.V. Influence of cell surface structures on crenarchaeal biofilm formation using a thermostable green fluorescent protein. Environ. Microbiol. 2012, 14, 779-793.
    • (2012) Environ. Microbiol. , vol.14 , pp. 779-793
    • Henche, A.L.1    Koerdt, A.2    Ghosh, A.3    Albers, S.V.4
  • 33
    • 78649679187 scopus 로고    scopus 로고
    • Crenarchaeal biofilm formation under extreme conditions
    • doi:10.1371/journal.pone.0014104
    • Koerdt, A.; Gödeke, J.; Berger, J.; Thormann, K.M.; Albers, S.V. Crenarchaeal biofilm formation under extreme conditions. PloS One 2010, doi:10.1371/journal.pone.0014104.
    • (2010) PloS One
    • Koerdt, A.1    Gödeke, J.2    Berger, J.3    Thormann, K.M.4    Albers, S.V.5
  • 37
    • 49749108549 scopus 로고    scopus 로고
    • An archaeal bi-species biofilm formed by Pyrococcus. furiosus and Methanopyrus. kandleri
    • Schopf, S.; Wanner, G.; Rachel, R.; Wirth, R. An archaeal bi-species biofilm formed by Pyrococcus. furiosus and Methanopyrus. kandleri. Arch. Microbiol. 2008, 190, 371-377.
    • (2008) Arch. Microbiol. , vol.190 , pp. 371-377
    • Schopf, S.1    Wanner, G.2    Rachel, R.3    Wirth, R.4
  • 38
    • 84888135079 scopus 로고    scopus 로고
    • Positive, neutral and negative interactions in cocultures between Pyrococcus. furiosus and different methanogenic Archaea
    • Weiner, A.; Schopf, S.; Wanner, G.; Probst, A.; Wirth, R. Positive, neutral and negative interactions in cocultures between Pyrococcus. furiosus and different methanogenic Archaea. Microb. Insights 2012, 5, 1-10.
    • (2012) Microb. Insights , vol.5 , pp. 1-10
    • Weiner, A.1    Schopf, S.2    Wanner, G.3    Probst, A.4    Wirth, R.5
  • 39
    • 84867092074 scopus 로고    scopus 로고
    • Regulation of archaella expression by the FHA and von Willebrand domain-containing proteins ArnA and ArnB in Sulfolobus. acidocaldarius
    • Reimann, J.; Lassak, K.; Khadouma, S.; Ettema, T.J.; Yang, N.; Driessen, A.J.; Klingl, A.; Albers, S.V. Regulation of archaella expression by the FHA and von Willebrand domain-containing proteins ArnA and ArnB in Sulfolobus. acidocaldarius. Mol. Microbiol. 2012, 86, 24-36.
    • (2012) Mol. Microbiol. , vol.86 , pp. 24-36
    • Reimann, J.1    Lassak, K.2    Khadouma, S.3    Ettema, T.J.4    Yang, N.5    Driessen, A.J.6    Klingl, A.7    Albers, S.V.8
  • 40
    • 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
  • 41
    • 0028182415 scopus 로고
    • Molecular analysis of archael flagellins: Similarity to the type IV pilin-transport superfamily widespread in bacteria
    • Faguy, D.M.; Jarrell, K.F.; Kuzio, J.; Kalmokoff, M.L. Molecular analysis of archael 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
  • 42
    • 0029835580 scopus 로고    scopus 로고
    • The archaeal flagellum: A unique motility structure
    • Jarrell, K.F.; Bayley, D.P.; Kostyukova, A.S. The archaeal flagellum: a unique motility structure. J. Bacteriol. 1996, 178, 5057-5064.
    • (1996) J. Bacteriol. , vol.178 , pp. 5057-5064
    • Jarrell, K.F.1    Bayley, D.P.2    Kostyukova, A.S.3
  • 43
    • 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
  • 44
    • 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. USA 1993, 90, 2404-2408.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2404-2408
    • Strom, M.S.1    Nunn, D.N.2    Lory, S.3
  • 45
    • 0043013091 scopus 로고    scopus 로고
    • Archaeal signal peptides-A comparative survey at the genome level
    • Bardy, S.L.; Eichler, J.; Jarrell, K.F. Archaeal signal peptides-A comparative survey at the genome level. Protein Sci. 2003, 12, 1833-1843.
    • (2003) Protein Sci. , vol.12 , pp. 1833-1843
    • Bardy, S.L.1    Eichler, J.2    Jarrell, K.F.3
  • 46
    • 0032014974 scopus 로고    scopus 로고
    • Further evidence to suggest that archaeal flagella are related to bacterial type IV pili
    • Bayley, D.P.; Jarrell, K.F. 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
  • 48
    • 0027938928 scopus 로고
    • Physical characterization of the flagella and flagellins from Methanospirillum. hungatei
    • Faguy, D.M.; Koval, S.F.; Jarrell, K.F. Physical characterization of the flagella and flagellins from Methanospirillum. hungatei. J. Bacteriol. 1994, 176, 7491-7498.
    • (1994) J. Bacteriol. , vol.176 , pp. 7491-7498
    • Faguy, D.M.1    Koval, S.F.2    Jarrell, K.F.3
  • 49
    • 0035105745 scopus 로고    scopus 로고
    • The archaeal flagellum: A different kind of prokaryotic motility structure
    • Thomas, N.A.; Bardy, S.L.; Jarrell, K.F. The archaeal flagellum: A different kind of prokaryotic motility structure. FEMS Microbiol. Rev. 2001, 25, 147-174.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 147-174
    • Thomas, N.A.1    Bardy, S.L.2    Jarrell, K.F.3
  • 51
    • 2642553801 scopus 로고    scopus 로고
    • Recent advances in the structure and assembly of the archaeal flagellum
    • Bardy, S.L.; Ng, S.Y.; Jarrell, K.F. 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
  • 52
    • 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.I.; 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.I.6    Jarrell, K.F.7
  • 53
    • 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
  • 54
    • 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
  • 55
    • 65349147066 scopus 로고    scopus 로고
    • Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus. maripaludis
    • Vandyke, D.J.; Wu, J.; Logan, S.M.; Kelly, J.F.; Mizuno, S.; Aizawa, S.I.; Jarrell, K.F. Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus. maripaludis. Mol. Microbiol. 2009, 72, 633-644.
    • (2009) Mol. Microbiol. , vol.72 , pp. 633-644
    • Vandyke, D.J.1    Wu, J.2    Logan, S.M.3    Kelly, J.F.4    Mizuno, S.5    Aizawa, S.I.6    Jarrell, K.F.7
  • 56
    • 79958134297 scopus 로고    scopus 로고
    • Role of N-linked glycosylation in cell surface structures of Archaea with a focus on flagella and S layers
    • doi: 10.1155/2010/470138
    • Jarrell, K.F.; Jones, G.M.; Nair, D.B. Role of N-linked glycosylation in cell surface structures of Archaea with a focus on flagella and S layers. Int. J. Microbiol. 2010, doi: 10.1155/2010/470138.
    • (2010) Int. J. Microbiol.
    • Jarrell, K.F.1    Jones, G.M.2    Nair, D.B.3
  • 57
    • 0024968229 scopus 로고
    • Halobacterial flagellins are encoded by a multigene family. Identification of all five gene products
    • Gerl, L.; Deutzmann, R.; Sumper, M. Halobacterial flagellins are encoded by a multigene family. Identification of all five gene products. FEBS Lett. 1989, 244, 137-140.
    • (1989) FEBS Lett. , vol.244 , pp. 137-140
    • Gerl, L.1    Deutzmann, R.2    Sumper, M.3
  • 58
    • 0024288620 scopus 로고
    • Halobacterial flagellins are encoded by a multigene family. Characterization of five flagellin genes
    • Gerl, L.; Sumper, M. Halobacterial flagellins are encoded by a multigene family. Characterization of five flagellin genes. J. Biol. Chem. 1988, 263, 13246-13251.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13246-13251
    • Gerl, L.1    Sumper, M.2
  • 60
    • 0023990563 scopus 로고
    • Isolation of flagella from the archaebacterium Methanococcus. voltae by phase separation with Triton X-114
    • Kalmokoff, M.L.; Jarrell, K.F.; Koval, S.F. 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
  • 61
    • 0036777348 scopus 로고    scopus 로고
    • Identification and localization of flagellins FlaA and FlaB3 within flagella of Methanococcus. voltae
    • Bardy, S.L.; Mori, T.; Komoriya, K.; Aizawa, S.; Jarrell, K.F. Identification and localization of flagellins FlaA and FlaB3 within 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.4    Jarrell, K.F.5
  • 62
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab, R.M. How bacteria assemble flagella. Annu. Rev. Microbiol. 2003, 57, 77-100.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 77-100
    • McNab, R.M.1
  • 63
    • 0030023488 scopus 로고    scopus 로고
    • Flagellar assembly in Salmonella typhimurium
    • Aizawa, S.I. Flagellar assembly in Salmonella typhimurium. Mol. Microbiol. 1996, 19, 1-5.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1-5
    • Aizawa, S.I.1
  • 64
    • 34548061787 scopus 로고    scopus 로고
    • On the multicomponent nature of Halobacterium. salinarum flagella
    • Beznosov, S.N.; Pyatibratov, M.G.; Fedorov, O.V. On the multicomponent nature of Halobacterium. salinarum flagella. Microbiology Russ. 2007, 76, 435-441.
    • (2007) Microbiology Russ. , vol.76 , pp. 435-441
    • Beznosov, S.N.1    Pyatibratov, M.G.2    Fedorov, O.V.3
  • 67
    • 0034633401 scopus 로고    scopus 로고
    • A novel pH2 control on the expression of flagella in the hyperthermophilic strictly hydrogenotrophic methanarchaeaon Methanococcus. jannaschii
    • Mukhopadhyay, B.; Johnson, E.F.; Wolfe, R.S. A novel pH2 control on the expression of flagella in the hyperthermophilic strictly hydrogenotrophic methanarchaeaon 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
  • 68
    • 0035213102 scopus 로고    scopus 로고
    • Characterization of flagellum gene families of methanogenic archaea and localization of novel flagellum accessory proteins
    • Thomas, N.A.; Jarrell, K.F. 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
  • 69
    • 84871593149 scopus 로고    scopus 로고
    • FlaX, a unique component of the crenarchaeal archaellum, forms oligomeric ring-shaped structures and interacts with the motor ATPase FlaI
    • Banerjee, A.; Ghosh, A.; Mills, D.J.; Kahnt, J.; Vonck, J.; Albers, S.V. FlaX, a unique component of the crenarchaeal archaellum, forms oligomeric ring-shaped structures and interacts with the motor ATPase FlaI. J. Biol. Chem. 2012, 287, 43322-43330.
    • (2012) J. Biol. Chem. , vol.287 , pp. 43322-43330
    • Banerjee, A.1    Ghosh, A.2    Mills, D.J.3    Kahnt, J.4    Vonck, J.5    Albers, S.V.6
  • 70
    • 79958838593 scopus 로고    scopus 로고
    • Archaeal flagellar ATPase motor shows ATP-dependent hexameric assembly and activity stimulation by specific lipid binding
    • Ghosh, A.; Hartung, S.; van der Does, C.; Tainer, J.A.; Albers, S.V. Archaeal flagellar ATPase motor shows ATP-dependent hexameric assembly and activity stimulation by specific lipid binding. Biochem. J. 2011, 437, 43-52.
    • (2011) Biochem. J. , vol.437 , pp. 43-52
    • Ghosh, A.1    Hartung, S.2    van der Does, C.3    Tainer, J.A.4    Albers, S.V.5
  • 71
    • 0025833831 scopus 로고
    • Cloning and sequencing of a multigene family encoding the flagellins of Methanococcus. voltae
    • Kalmokoff, M.L.; Jarrell, K.F. 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
  • 72
    • 32444431610 scopus 로고    scopus 로고
    • Active-site residues in the type IV prepilin peptidase homologue PibD from the archaeon Sulfolobus. solfataricus
    • Szabo, Z.; Albers, S.V.; Driessen, A.J.M. Active-site residues in the type IV prepilin peptidase homologue PibD from the archaeon Sulfolobus. solfataricus. J. Bacteriol. 2006, 188, 1437-1443.
    • (2006) J. Bacteriol. , vol.188 , pp. 1437-1443
    • Szabo, Z.1    Albers, S.V.2    Driessen, A.J.M.3
  • 73
    • 79960918054 scopus 로고    scopus 로고
    • The crystal structure of GxGD membrane protease FlaK
    • Hu, J.; Xue, Y.; Lee, S.; Ha, Y. The crystal structure of GxGD membrane protease FlaK. Nature 2011, 475, 528-531.
    • (2011) Nature , vol.475 , pp. 528-531
    • Hu, J.1    Xue, Y.2    Lee, S.3    Ha, Y.4
  • 74
    • 0035028932 scopus 로고    scopus 로고
    • Identification of amino acids in the leader peptide of Methanococcus. voltae preflagellin that are important in posttranslational processing
    • Thomas, N.A.; Chao, E.D.; Jarrell, K.F. Identification of amino acids in the leader peptide of Methanococcus. voltae preflagellin that are important in posttranslational processing. Arch. Microbiol. 2001, 175, 263-269.
    • (2001) Arch. Microbiol. , vol.175 , pp. 263-269
    • Thomas, N.A.1    Chao, E.D.2    Jarrell, K.F.3
  • 75
    • 70350462586 scopus 로고    scopus 로고
    • Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD
    • Ng, S.Y.; VanDyke, D.J.; Chaban, B.; Wu, J.; Nosaka, Y.; Aizawa, S.; Jarrell, K.F. Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD. J. Bacteriol. 2009, 191, 6732-6740.
    • (2009) J. Bacteriol. , vol.191 , pp. 6732-6740
    • Ng, S.Y.1    VanDyke, D.J.2    Chaban, B.3    Wu, J.4    Nosaka, Y.5    Aizawa, S.6    Jarrell, K.F.7
  • 76
    • 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
  • 77
    • 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, R.S.; Kelly, J.; Brisson, J.R.; Watson, D.; Bardy, S.L.; Jarrell, K.F.; Logan, S.M. Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus. voltae. J. Biol. Chem. 2005, 280, 16586-16593.
    • (2005) J. Biol. Chem. , vol.280 , 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
  • 78
    • 58149483373 scopus 로고    scopus 로고
    • AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus. voltae
    • Chaban, B.; Logan, S.M.; Kelly, J.F.; Jarrell, K.F. AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus. voltae. J. Bacteriol. 2009, 191, 187-195.
    • (2009) J. Bacteriol. , vol.191 , pp. 187-195
    • Chaban, B.1    Logan, S.M.2    Kelly, J.F.3    Jarrell, K.F.4
  • 79
    • 40449104807 scopus 로고    scopus 로고
    • Identification of the archaeal alg7 gene homolog encoding N-acetylglucosamine-1-phosphate transferase of the N-linked glycosylation system by cross-domain complementation in Saccharomyces. cerevisiae
    • Shams-Eldin, H.; Chaban, B.; Niehus, S.; Schwarz, R.T.; Jarrell, K.F. Identification of the archaeal alg7 gene homolog encoding N-acetylglucosamine-1-phosphate transferase of the N-linked glycosylation system by cross-domain complementation in Saccharomyces. cerevisiae. J. Bacteriol. 2008, 190, 2217-2220.
    • (2008) J. Bacteriol. , vol.190 , pp. 2217-2220
    • Shams-Eldin, H.1    Chaban, B.2    Niehus, S.3    Schwarz, R.T.4    Jarrell, K.F.5
  • 80
    • 41949094643 scopus 로고    scopus 로고
    • Acetamido sugar biosynthesis in the Euryarchaea
    • Namboori, S.C.; Graham, D.E. Acetamido sugar biosynthesis in the Euryarchaea. J. Bacteriol. 2008, 190, 2987-2996.
    • (2008) J. Bacteriol. , vol.190 , pp. 2987-2996
    • Namboori, S.C.1    Graham, D.E.2
  • 81
    • 84861398049 scopus 로고    scopus 로고
    • Identification of genes involved in the acetamidino group modification of the flagellin N-linked glycan of Methanococcus. maripaludis
    • Jones, G.M.; Wu, J.; Ding, Y.; Uchida, K.; Aizawa, S.; Robotham, A.; Logan, S.M.; Kelly, J.; Jarrell, K.F. Identification of genes involved in the acetamidino group modification of the flagellin N-linked glycan of Methanococcus. maripaludis. J. Bacteriol. 2012, 194, 2693-2702.
    • (2012) J. Bacteriol. , vol.194 , pp. 2693-2702
    • Jones, G.M.1    Wu, J.2    Ding, Y.3    Uchida, K.4    Aizawa, S.5    Robotham, A.6    Logan, S.M.7    Kelly, J.8    Jarrell, K.F.9
  • 82
    • 48149087089 scopus 로고    scopus 로고
    • Identification of 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.I.; Jarrell, K.F. Identification of 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.I.6    Jarrell, K.F.7
  • 83
    • 79960108098 scopus 로고    scopus 로고
    • Glyco-engineering in Archaea: Differential N-glycosylation of the S-layer glycoprotein in a transformed Haloferax. volcanii strain
    • Calo, D.; Guan, Z.; Eichler, J. Glyco-engineering in Archaea: differential N-glycosylation of the S-layer glycoprotein in a transformed Haloferax. volcanii strain. Microb. Biotechnol. 2011, 4, 461-470.
    • (2011) Microb. Biotechnol. , vol.4 , pp. 461-470
    • Calo, D.1    Guan, Z.2    Eichler, J.3
  • 84
    • 77955433290 scopus 로고    scopus 로고
    • Protein glycosylation in Archaea: Sweet and Extreme
    • Calo, D.; Kaminski, L.; Eichler, J. Protein glycosylation in Archaea: Sweet and Extreme. Glycobiology. 2010, 20, 1065-1076.
    • (2010) Glycobiology. , vol.20 , pp. 1065-1076
    • Calo, D.1    Kaminski, L.2    Eichler, J.3
  • 85
    • 84878989792 scopus 로고    scopus 로고
    • Post-translation modification in Archaea: Lessons from Haloferax. volcanii and other haloarchaea
    • doi: 10.1111/1574-6976.12012
    • Eichler, J.; Maupin-Furlow, J. Post-translation modification in Archaea: Lessons from Haloferax. volcanii and other haloarchaea. FEMS Microbiol. Rev. 2012, doi: 10.1111/1574-6976.12012.
    • (2012) FEMS Microbiol. Rev.
    • Eichler, J.1    Maupin-Furlow, J.2
  • 86
    • 36248931035 scopus 로고    scopus 로고
    • Haloferax. volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer
    • Abu-Qarn, M.; Yurist-Doutsch, S.; Giordano, A.; Trauner, A.; Morris, H.R.; Hitchen, P.; Medalia, O.; Dell, A.; Eichler, J. Haloferax. volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. J. Mol. Biol. 2007, 374, 1224-1236.
    • (2007) J. Mol. Biol. , vol.374 , pp. 1224-1236
    • Abu-Qarn, M.1    Yurist-Doutsch, S.2    Giordano, A.3    Trauner, A.4    Morris, H.R.5    Hitchen, P.6    Medalia, O.7    Dell, A.8    Eichler, J.9
  • 88
    • 68849088492 scopus 로고    scopus 로고
    • Quantitative proteomics of nutrient limitation in the hydrogenotrophic methanogen Methanococcus. maripaludis
    • Xia, Q.; Wang, T.; Hendrickson, E.L.; Lie, T.J.; Hackett, M.; Leigh, J.A. Quantitative proteomics of nutrient limitation in the hydrogenotrophic methanogen Methanococcus. maripaludis. BMC Microbiol. 2009, 9, 149.
    • (2009) BMC Microbiol. , vol.9 , pp. 149
    • Xia, Q.1    Wang, T.2    Hendrickson, E.L.3    Lie, T.J.4    Hackett, M.5    Leigh, J.A.6
  • 89
    • 79953161982 scopus 로고    scopus 로고
    • Characterization of the specific interaction between archael FHA domain-containing protein and the promoter of a flagella-like gene-cluster and its regulation by phosphorylation
    • Duan, X.; He, Z.G. Characterization of the specific interaction between archael FHA domain-containing protein and the promoter of a flagella-like gene-cluster and its regulation by phosphorylation. Biochem. Biophys. Res. Commun. 2011, 407, 242-247.
    • (2011) Biochem. Biophys. Res. Commun. , vol.407 , pp. 242-247
    • Duan, X.1    He, Z.G.2
  • 91
    • 0036384351 scopus 로고    scopus 로고
    • The structure of the archeabacterial 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 archeabacterial 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
  • 92
    • 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
  • 94
    • 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
  • 95
    • 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
  • 96
    • 0027517812 scopus 로고
    • Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria
    • Welch, M.; Oosawa, K.; Aizawa, S.; Eisenbach, M. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. PNAS 1993, 90, 8787-8791.
    • (1993) PNAS , vol.90 , pp. 8787-8791
    • Welch, M.1    Oosawa, K.2    Aizawa, S.3    Eisenbach, M.4
  • 98
    • 0342624740 scopus 로고    scopus 로고
    • Deletion analysis of the che operon in the archaeon Halobacterium. salinarium
    • Rudolph, J.; Oesterhelt, D. Deletion analysis 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
  • 99
    • 35448949028 scopus 로고    scopus 로고
    • Flagellation and chemotaxis
    • In Cavicchioli, R., Ed.; ASM Press: Washington, DC, USA
    • Jarrell, K.F.; Ng, S.Y.; Chaban, B. Flagellation and chemotaxis. In Cavicchioli, R., Ed.; Archaea: molecular and cellular biology; ASM Press: Washington, DC, USA, 2007; pp 385-410.
    • (2007) Archaea: Molecular and cellular biology , pp. 385-410
    • Jarrell, K.F.1    Ng, S.Y.2    Chaban, B.3
  • 100
    • 70450225036 scopus 로고    scopus 로고
    • The steady-state phase distribution of the motor switch complex model of Halobacterium. salinarum
    • del Rosario, R.C.; Diener, F.; Diener, M.; Oesterhelt, D. The steady-state phase distribution of the motor switch complex model of Halobacterium. salinarum. Math. Biosci. 2009, 222, 117-126.
    • (2009) Math. Biosci. , vol.222 , pp. 117-126
    • del Rosario, R.C.1    Diener, F.2    Diener, M.3    Oesterhelt, D.4
  • 101
    • 84857858107 scopus 로고    scopus 로고
    • Swimming behavior of selected species of Archaea
    • Herzog, B.; Wirth, R. Swimming behavior of selected species of Archaea. Appl. Environ. Microbiol. 2012, 78, 1670-1674.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 1670-1674
    • Herzog, B.1    Wirth, R.2
  • 102
    • 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
  • 103
    • 79958210527 scopus 로고    scopus 로고
    • Methanocaldococcus. villosus sp. nov., a heavily flagellated archaeon adhering to surfaces and forming cell-cell contacts
    • Bellack, A.; Huber, H.; Rachel, R.; Wanner, G.; Wirth, R. Methanocaldococcus. villosus sp. nov., a heavily flagellated archaeon adhering to surfaces and forming cell-cell contacts. Int. J. Syst. Evol. Microbiol. 2011, 61, 1239-1245.
    • (2011) Int. J. Syst. Evol. Microbiol. , vol.61 , pp. 1239-1245
    • Bellack, A.1    Huber, H.2    Rachel, R.3    Wanner, G.4    Wirth, R.5
  • 106
    • 0015811281 scopus 로고
    • Attachment of bacteria to sulfur in extreme environments
    • Weiss, R.L. Attachment of bacteria to sulfur in extreme environments. J. Gen. Microbiol. 1973, 77, 501-507.
    • (1973) J. Gen. Microbiol. , vol.77 , pp. 501-507
    • Weiss, R.L.1
  • 108
    • 84870705958 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa twitching motility: Type IV pili in action
    • Burrows, L.L. Pseudomonas aeruginosa twitching motility: type IV pili in action. Annu. Rev. Microbiol. 2012, 66, 493-520.
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 493-520
    • Burrows, L.L.1
  • 109
    • 42649085698 scopus 로고    scopus 로고
    • Type IV pili: E pluribus unum?
    • Pelicic, V. Type IV pili: e pluribus unum? Mol. Microbiol. 2008, 68, 827-837.
    • (2008) Mol. Microbiol. , vol.68 , pp. 827-837
    • Pelicic, V.1
  • 110
    • 51649115255 scopus 로고    scopus 로고
    • The Mth60-fimbriae of Methanothermobacter. thermoautotrophicus are functional adhesins
    • Thoma, C.; Frank, M.; Rachel, R.; Schmid, S.; Nather, D.; Wanner, G.; Wirth, R. The Mth60-fimbriae of Methanothermobacter. thermoautotrophicus are functional adhesins. Environ. Microbiol. 2008, 10, 2785-2795.
    • (2008) Environ. Microbiol. , vol.10 , pp. 2785-2795
    • Thoma, C.1    Frank, M.2    Rachel, R.3    Schmid, S.4    Nather, D.5    Wanner, G.6    Wirth, R.7
  • 112
    • 84874069696 scopus 로고    scopus 로고
    • Methanothermobacter. tenebrarum sp. nov., a hydrogenotrophic thermophilic methanogen isolated from gas-associated formation water of a natural gas field in Japan
    • doi:10.1099/ijs.0.041681-0
    • Nakamura, K.; Takahashi, A.; Mori, C.; Tamaki, H.; Mochimaru, H.; Nakamura, K.; Takamizawa, K.; Kamagata, Y. Methanothermobacter. tenebrarum sp. nov., a hydrogenotrophic thermophilic methanogen isolated from gas-associated formation water of a natural gas field in Japan. Int. J. Syst. Evol. Microbiol. 2012, doi:10.1099/ijs.0.041681-0.
    • (2012) Int. J. Syst. Evol. Microbiol.
    • Nakamura, K.1    Takahashi, A.2    Mori, C.3    Tamaki, H.4    Mochimaru, H.5    Nakamura, K.6    Takamizawa, K.7    Kamagata, Y.8
  • 113
    • 0035449036 scopus 로고    scopus 로고
    • Genes for tight adherence of Actinobacillus. actinomycetemcomitans: From plaque to plague to pond scum
    • Kachlany, S.C.; Planet, P.J.; DeSalle, R.; Fine, D.H.; Figurski, D.H. 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.C.1    Planet, P.J.2    DeSalle, R.3    Fine, D.H.4    Figurski, D.H.5
  • 114
    • 84886257275 scopus 로고    scopus 로고
    • Sa-Lrp from Sulfolobus. acidocaldarius is a versatile, glutamine-responsive, and architectural transcriptional regulator
    • doi: 10.1002/mbo3.58
    • Vassart, A.; van Wolferen, M.; Orell, A.; Hong, Y.; Peeters, E.; Albers, S.V.; Charlier, D. Sa-Lrp from Sulfolobus. acidocaldarius is a versatile, glutamine-responsive, and architectural transcriptional regulator. Microbiology Open 2012, doi: 10.1002/mbo3.58.
    • (2012) Microbiology Open
    • Vassart, A.1    van Wolferen, M.2    Orell, A.3    Hong, Y.4    Peeters, E.5    Albers, S.V.6    Charlier, D.7
  • 116
    • 84865727174 scopus 로고    scopus 로고
    • The unusual cell biology of the hyperthermophilic Crenarchaeon Ignicoccus. hospitalis
    • Huber, H.; Küper, U.; Daxer, S.; Rachel, R. The unusual cell biology of the hyperthermophilic Crenarchaeon Ignicoccus. hospitalis. Antonie. van Leeuwenhoek 2012, 102, 203-219.
    • (2012) Antonie. van Leeuwenhoek , vol.102 , pp. 203-219
    • Huber, H.1    Küper, U.2    Daxer, S.3    Rachel, R.4
  • 117
    • 79961096901 scopus 로고    scopus 로고
    • Proteomic characterization of cellular and molecular processes that enable the Nanoarchaeum. equitans-Ignicoccus. hospitalis relationship
    • doi:10.1371/journal.pone.0022942
    • Giannone, R.J.; Huber, H.; Karpinets, T.; Heimerl, T.; Küper, U.; Rachel, R.; Keller, M.; Hettich, R.L.; Podar, M. Proteomic characterization of cellular and molecular processes that enable the Nanoarchaeum. equitans-Ignicoccus. hospitalis relationship. PloS One 2011, doi:10.1371/journal.pone.0022942.
    • (2011) PloS One
    • Giannone, R.J.1    Huber, H.2    Karpinets, T.3    Heimerl, T.4    Küper, U.5    Rachel, R.6    Keller, M.7    Hettich, R.L.8    Podar, M.9
  • 118
    • 70349689931 scopus 로고    scopus 로고
    • Glycosyltransferases and oligosaccharyltransferases in Archaea: Putative components of the N-glycosylation pathway in the third domain of life
    • Magidovich, H.; Eichler, J. Glycosyltransferases and oligosaccharyltransferases in Archaea: putative components of the N-glycosylation pathway in the third domain of life. FEMS Microbiol. Lett. 2009, 300, 122-130.
    • (2009) FEMS Microbiol. Lett. , vol.300 , pp. 122-130
    • Magidovich, H.1    Eichler, J.2
  • 119
    • 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
  • 121
    • 0032816834 scopus 로고    scopus 로고
    • In vivo observation of cell division of anaerobic hyperthermophiles by using a high-intensity dark-field microscope
    • Horn, C.; Paulmann, B.; Kerlen, G.; Junker, N.; Huber, H. In vivo observation of cell division of anaerobic hyperthermophiles by using a high-intensity dark-field microscope. J. Bacteriol. 1999, 181, 5114-5118.
    • (1999) J. Bacteriol. , vol.181 , pp. 5114-5118
    • Horn, C.1    Paulmann, B.2    Kerlen, G.3    Junker, N.4    Huber, H.5
  • 122
    • 0036151763 scopus 로고    scopus 로고
    • Natural communities of novel archaea and bacteria with a string-of-pearls-like morphology: Molecular analysis of the bacterial partners
    • Moissl, C.; Rudolph, C.; Huber, R. Natural communities of novel archaea and bacteria with a string-of-pearls-like morphology: molecular analysis of the bacterial partners. Appl. Environ. Microbiol. 2002, 68, 933-937.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 933-937
    • Moissl, C.1    Rudolph, C.2    Huber, R.3
  • 124
    • 33644855188 scopus 로고    scopus 로고
    • New insights into the lifestyle of the cold-loving SM1 euryarchaeon: Natural growth as a monospecies biofilm in the subsurface
    • Henneberger, R.; Moissl, C.; Amann, T.; Rudolph, C.; Huber, R. New insights into the lifestyle of the cold-loving SM1 euryarchaeon: natural growth as a monospecies biofilm in the subsurface. Appl. Environ. Microbiol. 2006, 72, 192-199.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 192-199
    • Henneberger, R.1    Moissl, C.2    Amann, T.3    Rudolph, C.4    Huber, R.5
  • 125
    • 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
  • 126
    • 0035057117 scopus 로고    scopus 로고
    • Sugar transport in Sulfolobus. solfataricus is mediated by two families of binding protein-dependent ABC transporters
    • Elferink, M.G.; Albers, S.V.; Konings, W.N.; Driessen, A.J. Sugar transport in Sulfolobus. solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol. Microbiol. 2001, 39, 1494-1503.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1494-1503
    • Elferink, M.G.1    Albers, S.V.2    Konings, W.N.3    Driessen, A.J.4
  • 127
    • 79952244320 scopus 로고    scopus 로고
    • The bindosome is a structural component of the Sulfolobus. solfataricus cell envelope
    • Zolghadr, B.; Klingl, A.; Rachel, R.; Driessen, A.J.; Albers, S.V. The bindosome is a structural component of the Sulfolobus. solfataricus cell envelope. Extremophiles. 2011, 15, 235-244.
    • (2011) Extremophiles. , vol.15 , pp. 235-244
    • Zolghadr, B.1    Klingl, A.2    Rachel, R.3    Driessen, A.J.4    Albers, S.V.5
  • 128
    • 84870763465 scopus 로고    scopus 로고
    • Diversity, assembly and regulation of archaeal type IV pili-like and non-type-IV pili-like surface structures
    • Lassak, K.; Ghosh, A.; Albers, S.V. Diversity, assembly and regulation of archaeal type IV pili-like and non-type-IV pili-like surface structures. Res. Microbiol. 2012, 163, 630-644.
    • (2012) Res. Microbiol. , vol.163 , pp. 630-644
    • Lassak, K.1    Ghosh, A.2    Albers, S.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.