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Volumn 190, Issue 15, 2008, Pages 5300-5307

Identification of a putative acetyltransferase gene, MMP0350, which affects proper assembly of both flagella and pili in the archaeon Methanococcus maripaludis

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; FLAGELLIN; TRISACCHARIDE;

EID: 48149087089     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00474-08     Document Type: Article
Times cited : (39)

References (59)
  • 1
    • 33748517628 scopus 로고    scopus 로고
    • Protein N-glycosylation in Archaea: Defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation
    • Abu-Qarn, M., and J. Eichler. 2006. Protein N-glycosylation in Archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation. Mol. Microbiol. 61:511-525.
    • (2006) Mol. Microbiol , vol.61 , pp. 511-525
    • Abu-Qarn, M.1    Eichler, J.2
  • 2
    • 42549147096 scopus 로고    scopus 로고
    • Identification of AglE, a second glycosyltransferase involved in N-glycosylation of the Haloferax volcanii S-layer glycoprotein
    • Abu-Qarn, M., A. Giordano, F. Battaglia, A. Trauner, P. G. Hitchen, H. R. Morris, A. Dell, and J. Eichler. 2008. Identification of AglE, a second glycosyltransferase involved in N-glycosylation of the Haloferax volcanii S-layer glycoprotein. J. Bacteriol. 190:3140-3146.
    • (2008) J. Bacteriol , vol.190 , pp. 3140-3146
    • Abu-Qarn, M.1    Giordano, A.2    Battaglia, F.3    Trauner, A.4    Hitchen, P.G.5    Morris, H.R.6    Dell, A.7    Eichler, J.8
  • 3
    • 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., S. Yurist-Doutsch, A. Giordano, A. Trauner, H. R. Morris, P. Hitchen, O. Medalia, A. Dell, and J. Eichler. 2007. 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. 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
  • 4
    • 0023663381 scopus 로고
    • Biogenesis of E. coli Pap pili: PapH, a minor pilin subunit involved in cell anchoring and length modulation
    • Båga, M., M. Norgren, and S. Normark. 1987. Biogenesis of E. coli Pap pili: papH, a minor pilin subunit involved in cell anchoring and length modulation. Cell 49:241-251.
    • (1987) Cell , vol.49 , pp. 241-251
    • Båga, M.1    Norgren, M.2    Normark, S.3
  • 5
    • 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., and K. F. Jarrell. 2003. Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae. Mol. Microbiol. 50:1339-1347.
    • (2003) Mol. Microbiol , vol.50 , pp. 1339-1347
    • Bardy, S.L.1    Jarrell, K.F.2
  • 6
    • 0037133374 scopus 로고    scopus 로고
    • FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity
    • Bardy, S. L., and K. F. Jarrell. 2002. FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity. FEMS Microbiol. Lett. 208:53-59.
    • (2002) FEMS Microbiol. Lett , vol.208 , pp. 53-59
    • Bardy, S.L.1    Jarrell, K.F.2
  • 7
    • 0028785817 scopus 로고
    • Genetics in methanogens: Transposon insertion mutagenesis of a Methanococcus maripaludis nifH gene
    • Blank, C. E., P. S. Kessler, and J. A. Leigh. 1995. Genetics in methanogens: transposon insertion mutagenesis of a Methanococcus maripaludis nifH gene. J. Bacteriol. 177:5773-5777.
    • (1995) J. Bacteriol , vol.177 , pp. 5773-5777
    • Blank, C.E.1    Kessler, P.S.2    Leigh, J.A.3
  • 8
    • 0025832448 scopus 로고
    • Analysis and nucleotide sequence of the genes encoding the surface-layer glycoproteins of the hyperthermophilic methanogens Methanothermus fervidus and Methanothermus sociabilis
    • Bröckl, G., M. Behr, S. Fabry, R. Hensel, H. Kaudewitz, E. Biendl, and H. Konig. 1991. Analysis and nucleotide sequence of the genes encoding the surface-layer glycoproteins of the hyperthermophilic methanogens Methanothermus fervidus and Methanothermus sociabilis. Eur. J. Biochem. 199:147-152.
    • (1991) Eur. J. Biochem , vol.199 , pp. 147-152
    • Bröckl, G.1    Behr, M.2    Fabry, S.3    Hensel, R.4    Kaudewitz, H.5    Biendl, E.6    Konig, H.7
  • 9
    • 0035854812 scopus 로고    scopus 로고
    • Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan
    • Castric, P., F. J. Cassels, and R. W. Carlson. 2001. Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan. J. Biol. Chem. 276:26479-26485.
    • (2001) J. Biol. Chem , vol.276 , pp. 26479-26485
    • Castric, P.1    Cassels, F.J.2    Carlson, R.W.3
  • 10
    • 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., S. Voisin, J. Kelly, S. M. Logan, and K. F. Jarrell. 2006. 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. 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
  • 11
    • 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., S. Y. M. Ng, M. Kanbe, I. Saltzman, G. Nimmo, S. I. Aizawa, and K. F. Jarrell. 2007. 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. 66:596-609.
    • (2007) Mol. Microbiol , vol.66 , pp. 596-609
    • Chaban, B.1    Ng, S.Y.M.2    Kanbe, M.3    Saltzman, I.4    Nimmo, G.5    Aizawa, S.I.6    Jarrell, K.F.7
  • 12
    • 37449032773 scopus 로고    scopus 로고
    • The flagellar filament structure of the extreme acidothermophile Sulfolobus shibatae B12 suggests that archaebacterial flagella have a unique and common symmetry and design
    • Cohen-Krausz, S., and S. Trachtenberg. 2008. The flagellar filament structure of the extreme acidothermophile Sulfolobus shibatae B12 suggests that archaebacterial flagella have a unique and common symmetry and design. J. Mol. Biol. 375:1113-1124.
    • (2008) J. Mol. Biol , vol.375 , pp. 1113-1124
    • Cohen-Krausz, S.1    Trachtenberg, S.2
  • 14
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in Archaea
    • Eichler, J., and M. W. Adams. 2005. Posttranslational protein modification in Archaea. Microbiol. Mol. Biol. Rev. 69:393-425.
    • (2005) Microbiol. Mol. Biol. Rev , vol.69 , pp. 393-425
    • Eichler, J.1    Adams, M.W.2
  • 15
    • 0031965752 scopus 로고    scopus 로고
    • Structure and expression of the FlaA periplasmic flagellar protein of Borrelia burgdorferi
    • Ge, Y., C. Li, L. Corum, C. A. Slaughter, and N. W. Charon. 1998. Structure and expression of the FlaA periplasmic flagellar protein of Borrelia burgdorferi. J. Bacteriol. 180:2418-2425.
    • (1998) J. Bacteriol , vol.180 , pp. 2418-2425
    • Ge, Y.1    Li, C.2    Corum, L.3    Slaughter, C.A.4    Charon, N.W.5
  • 16
    • 0025305971 scopus 로고
    • Construction of an integration vector for use in the archacbacterium Methanococcus voltae and expression of a eubacterial resistance gene
    • Gernhardt, P., O. Possot, M. Foglino, L. Sibold, and A. Klein. 1990. Construction of an integration vector for use in the archacbacterium Methanococcus voltae and expression of a eubacterial resistance gene. Mol. Gen. Genet. 221:273-279.
    • (1990) Mol. Gen. Genet , vol.221 , pp. 273-279
    • Gernhardt, P.1    Possot, O.2    Foglino, M.3    Sibold, L.4    Klein, A.5
  • 17
    • 0024351039 scopus 로고
    • Phenotypic characterization of the archaebacterial genus Sulfolobus: Comparison of five wild-type strains
    • Grogan, D. W. 1989. Phenotypic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains. J Bacteriol. 171:6710-6719.
    • (1989) J Bacteriol , vol.171 , pp. 6710-6719
    • Grogan, D.W.1
  • 18
    • 35448949028 scopus 로고    scopus 로고
    • Flagellation and chemotaxis
    • R. Cavicchioli ed, ASM Press, Washington, DC
    • Jarrell, K. F., S. Y. M. Ng, and B. Chaban. 2007. Flagellation and chemotaxis, p. 385-410. In R. Cavicchioli (ed.), Archaea: molecular and cellular biology. ASM Press, Washington, DC.
    • (2007) Archaea: Molecular and cellular biology , pp. 385-410
    • Jarrell, K.F.1    Ng, S.Y.M.2    Chaban, B.3
  • 19
    • 0029835580 scopus 로고    scopus 로고
    • The archaeal flagellum: A unique motility structure
    • Jarrell, K. F., D. P. Bayley, and A. S. Kostyukova. 1996. The archaeal flagellum: a unique motility structure. J. Bacteriol. 178:5057-5064.
    • (1996) J. Bacteriol , vol.178 , pp. 5057-5064
    • Jarrell, K.F.1    Bayley, D.P.2    Kostyukova, A.S.3
  • 21
    • 0017394692 scopus 로고
    • Methanococcus vannielii: Ultrastructure and sensitivity to detergents and antibiotics
    • Jones, J. B., B. Bowers, and T. C. Stadtman. 1977. Methanococcus vannielii: ultrastructure and sensitivity to detergents and antibiotics. J. Bacteriol. 130:1357-1363.
    • (1977) J. Bacteriol , vol.130 , pp. 1357-1363
    • Jones, J.B.1    Bowers, B.2    Stadtman, T.C.3
  • 22
    • 0002620715 scopus 로고
    • Characterization of Methanococcus maripaludis sp. nov., a new methanogen isolated from salt marsh sediment
    • Jones, W. J., M. J. B. Paynter, and R. Gupta. 1983. Characterization of Methanococcus maripaludis sp. nov., a new methanogen isolated from salt marsh sediment. Arch. Microbiol. 135:91-97.
    • (1983) Arch. Microbiol , vol.135 , pp. 91-97
    • Jones, W.J.1    Paynter, M.J.B.2    Gupta, R.3
  • 24
    • 33645228374 scopus 로고    scopus 로고
    • Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer
    • Kelly, J., H. Jarrell, L. Millar, L. Tessier, L. M. Fiori, P. C. Lau, B. Allan, and C. M. Szymanski. 2006. Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer. J. Bacteriol. 188:2427-2434.
    • (2006) J. Bacteriol , vol.188 , pp. 2427-2434
    • Kelly, J.1    Jarrell, H.2    Millar, L.3    Tessier, L.4    Fiori, L.M.5    Lau, P.C.6    Allan, B.7    Szymanski, C.M.8
  • 25
    • 0023131538 scopus 로고
    • Ultrastructure and biochemistry of the cell wall of Methanococcus voltae
    • Koval, S. F., and K. F. Jarrell. 1987. Ultrastructure and biochemistry of the cell wall of Methanococcus voltae. J. Bacteriol. 169:1298- 1306.
    • (1987) J. Bacteriol , vol.169 , pp. 1298-1306
    • Koval, S.F.1    Jarrell, K.F.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0027146367 scopus 로고
    • A species-specific periplasmic flagellar protein of Serpulina (Treponema) hyodysenteriae
    • Li, Z., F. Dumas, D. Dubreuil, and M. Jacques. 1993. A species-specific periplasmic flagellar protein of Serpulina (Treponema) hyodysenteriae. J. Bacteriol. 175:8000-8007.
    • (1993) J. Bacteriol , vol.175 , pp. 8000-8007
    • Li, Z.1    Dumas, F.2    Dubreuil, D.3    Jacques, M.4
  • 28
    • 0036777897 scopus 로고    scopus 로고
    • Regulatory response of Methanococcus maripaludis to alanine, an intermediate nitrogen source
    • Lie, T. J., and J. A. Leigh. 2002. Regulatory response of Methanococcus maripaludis to alanine, an intermediate nitrogen source. J. Bacteriol. 184:5301-5306.
    • (2002) J. Bacteriol , vol.184 , pp. 5301-5306
    • Lie, T.J.1    Leigh, J.A.2
  • 29
    • 14044255851 scopus 로고    scopus 로고
    • Regulation of nif expression in Methanococcus maripaludis: Roles of the euryarchaeal repressor NrpR, 2-oxoglutarate, and two operators
    • Lie, T. J., G. E. Wood, and J. A. Leigh. 2005. Regulation of nif expression in Methanococcus maripaludis: roles of the euryarchaeal repressor NrpR, 2-oxoglutarate, and two operators. J. Biol. Chem. 280:5236-5241.
    • (2005) J. Biol. Chem , vol.280 , pp. 5236-5241
    • Lie, T.J.1    Wood, G.E.2    Leigh, J.A.3
  • 30
    • 33646757219 scopus 로고    scopus 로고
    • Flagellar glycosylation - a new component of the motility repertoire?
    • Logan, S. M. 2006. Flagellar glycosylation - a new component of the motility repertoire? Microbiology 152:1249-1262.
    • (2006) Microbiology , vol.152 , pp. 1249-1262
    • Logan, S.M.1
  • 31
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab, R. M. 2003. How bacteria assemble flagella. Annu. Rev. Microbiol. 57:77-100.
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 32
    • 0017278612 scopus 로고
    • Purification and characterization of a prokaryotic glucoprotein from the cell envelope of Halobacterium salinarium
    • Mescher, M. F., and J. L. Strominger. 1976. Purification and characterization of a prokaryotic glucoprotein from the cell envelope of Halobacterium salinarium. J. Biol. Chem. 251:2005-2014.
    • (1976) J. Biol. Chem , vol.251 , pp. 2005-2014
    • Mescher, M.F.1    Strominger, J.L.2
  • 33
    • 0016123083 scopus 로고
    • Protein and carbohydrate composition of the cell envelope of Halobacterium salinarium
    • Mescher, M. F., J. L. Strominger, and S. W. Watson. 1974. Protein and carbohydrate composition of the cell envelope of Halobacterium salinarium. J. Bacteriol. 120:945-954.
    • (1974) J. Bacteriol , vol.120 , pp. 945-954
    • Mescher, M.F.1    Strominger, J.L.2    Watson, S.W.3
  • 34
    • 13244269794 scopus 로고    scopus 로고
    • Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease
    • Moore, B. C., and J. A. Leigh. 2005. Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease. J. Bacteriol. 187:972-979.
    • (2005) J. Bacteriol , vol.187 , pp. 972-979
    • Moore, B.C.1    Leigh, J.A.2
  • 35
    • 41949094643 scopus 로고    scopus 로고
    • Acetamido sugar biosynthesis in the Euryarchaea
    • Namboori, S. C., and D. E. Graham. 2008. Acetamido sugar biosynthesis in the Euryarchaea. J. Bacteriol. 190:2987-2996.
    • (2008) J. Bacteriol , vol.190 , pp. 2987-2996
    • Namboori, S.C.1    Graham, D.E.2
  • 36
    • 48149085143 scopus 로고    scopus 로고
    • Ng, S. Y. M., M. Kanbe, S.-I. Aizawa, and K. F. Jarrell. 2007. Isolation and characterization of pili from the archaeon Methanococcus maripaludis, abstr. I-005, p. 341-342. Abstr. 107th Gen. Meet. Am. Soc. Microbiol. American Society for Microbiology, Washington, DC.
    • Ng, S. Y. M., M. Kanbe, S.-I. Aizawa, and K. F. Jarrell. 2007. Isolation and characterization of pili from the archaeon Methanococcus maripaludis, abstr. I-005, p. 341-342. Abstr. 107th Gen. Meet. Am. Soc. Microbiol. American Society for Microbiology, Washington, DC.
  • 37
    • 33748757929 scopus 로고    scopus 로고
    • Archaeal flagella, bacterial flagella and type IV pili: A comparison of genes and posttranslational modifications
    • Ng, S. Y. M., B. Chaban, and K. F. Jarrell. 2006. Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications. J. Mol. Microbiol. Biotechnol. 11:167-191.
    • (2006) J. Mol. Microbiol. Biotechnol , vol.11 , pp. 167-191
    • Ng, S.Y.M.1    Chaban, B.2    Jarrell, K.F.3
  • 38
    • 48149097572 scopus 로고    scopus 로고
    • Nobbs, A. H., R. Rosini, D. Maione, G. Grandi, and J. L. Telford. 2007. Sortase A, together with a pilus island sortase C, is required for efficient cell wall attachment of pili in Streptococcus agalactiae, abstr. D-062, p. 232-233. Abstr. 107th Gen. Meet. Am. Soc. Microbiol. American Society for Microbiology, Washington, DC.
    • Nobbs, A. H., R. Rosini, D. Maione, G. Grandi, and J. L. Telford. 2007. Sortase A, together with a pilus island sortase C, is required for efficient cell wall attachment of pili in Streptococcus agalactiae, abstr. D-062, p. 232-233. Abstr. 107th Gen. Meet. Am. Soc. Microbiol. American Society for Microbiology, Washington, DC.
  • 39
    • 0345306190 scopus 로고    scopus 로고
    • Peabody, C. R., Y. J. Chung, M. R. Yen, D. Vidal-Ingigliardi, A. P. Pugsley, and M. H. Saier, Jr. 2003. Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. Microbiology 149:3051-3072.
    • Peabody, C. R., Y. J. Chung, M. R. Yen, D. Vidal-Ingigliardi, A. P. Pugsley, and M. H. Saier, Jr. 2003. Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. Microbiology 149:3051-3072.
  • 43
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: Glycoproteins in bacterial pathogens
    • Schmidt, M. A., L. W. Riley, and I. Benz. 2003. Sweet new world: glycoproteins in bacterial pathogens. Trends Microbiol. 11:554-561.
    • (2003) Trends Microbiol , vol.11 , pp. 554-561
    • Schmidt, M.A.1    Riley, L.W.2    Benz, I.3
  • 44
    • 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., B. Chaban, S. Niehus, R. T. Schwarz, and K. F. Jarrell. 2008. 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. 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
  • 47
    • 0023235232 scopus 로고
    • Halobacterial glycoprotein biosynthesis
    • Sumper, M. 1987. Halobacterial glycoprotein biosynthesis. Biochim. Biophys. Acta 906:69-79.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 69-79
    • Sumper, M.1
  • 48
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper, M., E. Berg, R. Mengele, and I. Strobel. 1990. Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. J. Bacteriol. 172:7111-7118.
    • (1990) J. Bacteriol , vol.172 , pp. 7111-7118
    • Sumper, M.1    Berg, E.2    Mengele, R.3    Strobel, I.4
  • 49
    • 33846567505 scopus 로고    scopus 로고
    • Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases
    • Szabó, Z., A. O. Stahl, S. V. Albers, J. C. Kissinger, A. J. Driessen, and M. Pohlschroder. 2007. Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases. J. Bacteriol. 189:772-778.
    • (2007) J. Bacteriol , vol.189 , pp. 772-778
    • Szabó, Z.1    Stahl, A.O.2    Albers, S.V.3    Kissinger, J.C.4    Driessen, A.J.5    Pohlschroder, M.6
  • 50
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski, C. M., and B. W. Wren. 2005. Protein glycosylation in bacterial mucosal pathogens. Nat. Rev. Microbiol. 3:225-237.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 225-237
    • Szymanski, C.M.1    Wren, B.W.2
  • 51
    • 0037674764 scopus 로고    scopus 로고
    • Campylobacter - a tale of two protein glycosylation systems
    • Szymanski, C. M., S. M. Logan, D. Linton, and B. W. Wren. 2003. Campylobacter - a tale of two protein glycosylation systems. Trends Microbiol. 11:233-238.
    • (2003) Trends Microbiol , vol.11 , pp. 233-238
    • Szymanski, C.M.1    Logan, S.M.2    Linton, D.3    Wren, B.W.4
  • 52
    • 0034888193 scopus 로고    scopus 로고
    • Insertional inactivation of the flaH gene in the archaeon Methanococcus voltae results in non-flagellated cells
    • Thomas, N. A., C. T. Pawson, and K. F. Jarrell. 2001. Insertional inactivation of the flaH gene in the archaeon Methanococcus voltae results in non-flagellated cells. Mol. Genet. Genomics 265:596-603.
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 596-603
    • Thomas, N.A.1    Pawson, C.T.2    Jarrell, K.F.3
  • 53
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 54
    • 33748768732 scopus 로고    scopus 로고
    • The archaeabacterial flagellar filament: A bacterial propeller with a pilus-like structure
    • Trachtenberg, S., and S. Cohen-Krausz. 2006. The archaeabacterial flagellar filament: a bacterial propeller with a pilus-like structure. J. Mol. Microbiol. Biotechnol. 11:208-220.
    • (2006) J. Mol. Microbiol. Biotechnol , vol.11 , pp. 208-220
    • Trachtenberg, S.1    Cohen-Krausz, S.2
  • 55
    • 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., R. S. Houliston, J. Kelly, J. R. Brisson, D. Watson, S. L. Bardy, K. F. Jarrell, and S. M. Logan. 2005. Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae. J. Biol. Chem. 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
  • 56
    • 0031061543 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene encoding the cell surface glycoprotein of Haloarcula japonica strain TR-1
    • Wakai, H., S. Nakamura, H. Kawasaki, K. Takada, S. Mizutani, R. Aono, and K. Horikoshi. 1997. Cloning and sequencing of the gene encoding the cell surface glycoprotein of Haloarcula japonica strain TR-1. Extremophiles 1:29-35.
    • (1997) Extremophiles , vol.1 , pp. 29-35
    • Wakai, H.1    Nakamura, S.2    Kawasaki, H.3    Takada, K.4    Mizutani, S.5    Aono, R.6    Horikoshi, K.7
  • 57
    • 0028170351 scopus 로고
    • Characterization of a gene, pilU, required for twitching motility but not phage sensitivity in Pseudomonas aeruginosa
    • Whitchurch, C. B., and J. S. Mattick. 1994. Characterization of a gene, pilU, required for twitching motility but not phage sensitivity in Pseudomonas aeruginosa. Mol. Microbiol. 13:1079-1091.
    • (1994) Mol. Microbiol , vol.13 , pp. 1079-1091
    • Whitchurch, C.B.1    Mattick, J.S.2
  • 58
    • 0024120902 scopus 로고
    • Structure and biosynthesis of prokaryotic glycoproteins
    • Wieland, F. 1988. Structure and biosynthesis of prokaryotic glycoproteins. Biochimie 70:1493-1504.
    • (1988) Biochimie , vol.70 , pp. 1493-1504
    • Wieland, F.1


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