메뉴 건너뛰기




Volumn 3, Issue JUL, 2012, Pages

Diversity and subcellular distribution of archaeal secreted proteins

Author keywords

Archaea; Archaeosortase; Cell surface structures; Lipoprotein; Pili; Protein transport; Sec transport; Tat transport

Indexed keywords


EID: 84875766625     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2012.00207     Document Type: Article
Times cited : (23)

References (143)
  • 2
    • 0032984481 scopus 로고    scopus 로고
    • A unique short signal sequence in membrane-anchored proteins of archaea
    • Albers, S. V., Konings, W. N., and Driessen, A. J. M. (1999). A unique short signal sequence in membrane-anchored proteins of archaea. Mol. Microbiol. 31, 1595-1596.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1595-1596
    • Albers, S.V.1    Konings, W.N.2    Driessen, A.J.M.3
  • 4
    • 67349199521 scopus 로고    scopus 로고
    • Diversity of archaeal type IV pilin-like structures
    • Albers, S. V., and Pohlschroder, M. (2009). Diversity of archaeal type IV pilin-like structures. Extremophiles 13,403-410.
    • (2009) Extremophiles , vol.13 , pp. 403-410
    • Albers, S.V.1    Pohlschroder, M.2
  • 5
    • 0038170287 scopus 로고    scopus 로고
    • Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity
    • Albers, S.V., Szabo,Z., and Driessen, A. J. (2003). Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity. J. Bacteriol. 185,3918-3925.
    • (2003) J. Bacteriol. , vol.185 , pp. 3918-3925
    • Albers, S.V.1    Szabo, Z.2    Driessen, A.J.3
  • 6
    • 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., and Koster, M. (2007). Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II secretion system via the signal recognition particle-Sec pathway. J. Bacteriol. 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
  • 7
    • 61549096272 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-positive bacteria with a hidden Markov model
    • Bagos, P. G., Tsirigos, K. D., Liakopoulos, T. D., and Hamodrakas, S. J. (2008). Prediction of lipoprotein signal peptides in Gram-positive bacteria with a hidden Markov model. J. Proteome Res. 7, 5082-5093.
    • (2008) J. Proteome Res. , vol.7 , pp. 5082-5093
    • Bagos, P.G.1    Tsirigos, K.D.2    Liakopoulos, T.D.3    Hamodrakas, S.J.4
  • 9
    • 78751502214 scopus 로고    scopus 로고
    • Structural and functional insights into Aeropyrum pernix OppA, a member of a novel archaeal OppA subfamily
    • Balestrieri, M., Gogliettino, M., Fiume, I., Pocsfalvi, G., Catara, G., Rossi, M., and Palmieri, G. (2011). Structural and functional insights into Aeropyrum pernix OppA, a member of a novel archaeal OppA subfamily. J. Bacteriol. 193,620-630.
    • (2011) J. Bacteriol. , vol.193 , pp. 620-630
    • Balestrieri, M.1    Gogliettino, M.2    Fiume, I.3    Pocsfalvi, G.4    Catara, G.5    Rossi, M.6    Palmieri, G.7
  • 10
    • 0043013091 scopus 로고    scopus 로고
    • Archaeal signal peptides - a comparative survey at the genome level
    • Bardy, S. L., Eichler, J., and Jarrell, K. F. (2003). Archaeal signal peptides - a comparative survey at the genome level. Protein Sci. 12, 1833-1843.
    • (2003) Protein Sci , vol.12 , pp. 1833-1843
    • Bardy, S.L.1    Eichler, J.2    Jarrell, K.F.3
  • 11
    • 0037133374 scopus 로고    scopus 로고
    • FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity
    • Bardy, S. L., and Jarrell, K. F. (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
  • 12
    • 84155180701 scopus 로고    scopus 로고
    • Cyclodextrin glycosyltransferase: a key enzyme in the assimilation of starch by the halophilic archaeon Haloferax mediterranei
    • Bautista, V., Esclapez, J., Perez-Pomares, E, Martinez-Espinosa, R. M., Camacho, M., and Bonete, M. J. (2012). Cyclodextrin glycosyltransferase: a key enzyme in the assimilation of starch by the halophilic archaeon Haloferax mediterranei. Extremophiles 16, 147-159.
    • (2012) Extremophiles , vol.16 , pp. 147-159
    • Bautista, V.1    Esclapez, J.2    Perez-Pomares, E.3    Martinez-Espinosa, R.M.4    Camacho, M.5    Bonete, M.J.6
  • 14
    • 15744405122 scopus 로고    scopus 로고
    • Protein targeting by the bacterial twin-arginine translocation (Tat) pathway
    • Berks, B. C., Palmer, T., and Sargent, F. (2005). Protein targeting by the bacterial twin-arginine translocation (Tat) pathway. Curr. Opin. Microbiol. 8, 174-181.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 174-181
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 15
    • 0036854430 scopus 로고    scopus 로고
    • Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway?
    • Bolhuis, A. (2002). Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway? Microbiology 148, 3335-3346.
    • (2002) Microbiology , vol.148 , pp. 3335-3346
    • Bolhuis, A.1
  • 16
    • 33747334086 scopus 로고    scopus 로고
    • The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity
    • doi:10.1186/1471-2164-7-169
    • Bolhuis, H., Palm, P., Wende, A., Falb, M., Rampp, M., Rodriguez-Valera, F., Pfeiffer, F., and Oesterhelt, D. (2006). The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity. BMC Genomics 7,169. doi:10.1186/1471-2164-7-169
    • (2006) BMC Genomics , vol.7 , pp. 169
    • Bolhuis, H.1    Palm, P.2    Wende, A.3    Falb, M.4    Rampp, M.5    Rodriguez-Valera, F.6    Pfeiffer, F.7    Oesterhelt, D.8
  • 17
    • 0025832448 scopus 로고
    • Analysis and nucleotide sequence of the genes encoding the surface-layer glyco-proteins of the hyperthermophilic methanogens Methanothermus fervidus and Methanothermus sociabilis
    • Brockl, G., Behr, M., Fabry, S., Hensel, R., Kaudewitz, H., Biendl, E., and Konig, H. (1991). Analysis and nucleotide sequence of the genes encoding the surface-layer glyco-proteins of the hyperthermophilic methanogens Methanothermus fervidus and Methanothermus sociabilis. Eur. I Biochem. 199, 147-152.
    • (1991) Eur. I Biochem. , vol.199 , pp. 147-152
    • Brockl, G.1    Behr, M.2    Fabry, S.3    Hensel, R.4    Kaudewitz, H.5    Biendl, E.6    Konig, H.7
  • 19
    • 79851507992 scopus 로고    scopus 로고
    • Crossing the membrane in archaea, the third domain of life
    • Calo, D., and Eichler, J. (2011). Crossing the membrane in archaea, the third domain of life. Biochim. Biophys. Acta 1808, 885-891.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 885-891
    • Calo, D.1    Eichler, J.2
  • 20
    • 77955433290 scopus 로고    scopus 로고
    • Protein glycosylation in archaea: sweet and extreme
    • Calo, D., Kaminski, L., and Eichler, J. (2010). Protein glycosylation in archaea: sweet and extreme. Glycobiology 20, 1065-1076.
    • (2010) Glycobiology , vol.20 , pp. 1065-1076
    • Calo, D.1    Kaminski, L.2    Eichler, J.3
  • 21
    • 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. M., Kanbe, M., Saltzman, L., Nimmo, G., Aizawa, S. I., and Jarrell, K. E (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, L.4    Nimmo, G.5    Aizawa, S.I.6    Jarrell, K.E.7
  • 22
    • 0031036328 scopus 로고    scopus 로고
    • Isolation, sequence, and expression of the gene encoding halocin H4, a bacteriocin from the halophilic archaeon Haloferax mediterranei R4
    • Cheung, J., Danna, K. J., O'Connor, E. M., Price, L. B., and Shand, R. E (1997). Isolation, sequence, and expression of the gene encoding halocin H4, a bacteriocin from the halophilic archaeon Haloferax mediterranei R4. J. Bacteriol. 179, 548-551.
    • (1997) J. Bacteriol. , vol.179 , pp. 548-551
    • Cheung, J.1    Danna, K.J.2    O'Connor, E.M.3    Price, L.B.4    Shand, R.E.5
  • 23
    • 26844547984 scopus 로고    scopus 로고
    • Identification and characterization of the Sulfolobus solfataricus P2 proteome
    • Chong, P. K., and Wright, P. C. (2005). Identification and characterization of the Sulfolobus solfataricus P2 proteome. J. Proteome Res. 4, 1789-1798.
    • (2005) J. Proteome Res. , vol.4 , pp. 1789-1798
    • Chong, P.K.1    Wright, P.C.2
  • 24
    • 84857548626 scopus 로고    scopus 로고
    • Conserved signal peptide recognition systems across the prokaryotic domains
    • Coulthurst, S. J., Dawson, A., Hunter, W. N., and Sargent, E (2012). Conserved signal peptide recognition systems across the prokaryotic domains. Biochemistry 51, 1678-1686.
    • (2012) Biochemistry , vol.51 , pp. 1678-1686
    • Coulthurst, S.J.1    Dawson, A.2    Hunter, W.N.3    Sargent, E.4
  • 25
  • 26
    • 50649105260 scopus 로고    scopus 로고
    • Gene cloning and heterologous synthesis of a haloalkaliphilic extracellular protease of Natrialba magadii (Nep)
    • De Castro, R. E., Ruiz, D. M., Gimenez, M. I., Silveyra, M. X., Paggi, R. A., and Maupin-Furlow, J. A. (2008). Gene cloning and heterologous synthesis of a haloalkaliphilic extracellular protease of Natrialba magadii (Nep). Extremophiles 12, 677-687.
    • (2008) Extremophiles , vol.12 , pp. 677-687
    • De Castro, R.E.1    Ruiz, D.M.2    Gimenez, M.I.3    Silveyra, M.X.4    Paggi, R.A.5    Maupin-Furlow, J.A.6
  • 27
    • 0035141976 scopus 로고    scopus 로고
    • Purification, characterization, and molecular modeling of pyrolysin and other extracellular thermostable serine proteases from hyperthermophilic microorganisms
    • deVos,W.M.,Voorhorst,W. G.B.,Dijkgraaf, M., Kluskens, L. D., Van Der Oost, J., and Siezen, R. J. (2001). Purification, characterization, and molecular modeling of pyrolysin and other extracellular thermostable serine proteases from hyperthermophilic microorganisms. Methods Enzymol. 330, 383-393.
    • (2001) Methods Enzymol , vol.330 , pp. 383-393
    • deVos, W.M.1    Voorhorst, W.G.B.2    Dijkgraaf, M.3    Kluskens, L.D.4    Van Der Oost, J.5    Siezen, R.J.6
  • 28
    • 27844443566 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea
    • Dilks, K., Gimenez, M. I., and Pohlschroder, M. (2005). Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea. J. Bacteriol. 187,8104-8113.
    • (2005) J. Bacteriol. , vol.187 , pp. 8104-8113
    • Dilks, K.1    Gimenez, M.I.2    Pohlschroder, M.3
  • 29
    • 0037317124 scopus 로고    scopus 로고
    • Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey
    • Dilks, K., Rose, R. W., Hartmann, E., and Pohlschroder, M. (2003). Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey.J. Bacteriol. 185, 1478-1483.
    • (2003) J. Bacteriol. , vol.185 , pp. 1478-1483
    • Dilks, K.1    Rose, R.W.2    Hartmann, E.3    Pohlschroder, M.4
  • 30
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen, A. J., and Nouwen, N. (2008). Protein translocation across the bacterial cytoplasmic membrane. Annu. Rev. Biochem. 77, 643-667.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 31
  • 32
    • 0036176704 scopus 로고    scopus 로고
    • Archaeal signal peptidases from the genus Thermoplasma: structural and mechanistic hybrids of the bacterial and eukaryal enzymes
    • Eichler, J. (2002). Archaeal signal peptidases from the genus Thermoplasma: structural and mechanistic hybrids of the bacterial and eukaryal enzymes. J. Mol Evol. 54, 411-415.
    • (2002) J. Mol Evol. , vol.54 , pp. 411-415
    • Eichler, J.1
  • 33
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in archaea
    • Eichler, J., and Adams, M. W. (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
  • 34
    • 0035057117 scopus 로고    scopus 로고
    • Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters
    • Elferink, M. G. L., Albers, S. V., Konings, W. N., and Driessen, A. J. M. (2001). Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol. Microbiol. 39,1494-1503.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1494-1503
    • Elferink, M.G.L.1    Albers, S.V.2    Konings, W.N.3    Driessen, A.J.M.4
  • 35
    • 72449192318 scopus 로고    scopus 로고
    • Comparative study of the extracellular proteome of Sulfolobus species reveals limited secretion
    • Ellen, A. F., Albers, S. V., and Driessen, A. J. (2010a). Comparative study of the extracellular proteome of Sulfolobus species reveals limited secretion. Extremophiles 14, 87-98.
    • (2010) Extremophiles , vol.14 , pp. 87-98
    • Ellen, A.F.1    Albers, S.V.2    Driessen, A.J.3
  • 38
    • 80052324393 scopus 로고    scopus 로고
    • The sulfolobicin genes of Sulfolobus acidocaldarius encode novel antimicrobial proteins
    • Ellen, A. F., Rohulya, O. V., Fusetti, E, Wagner, M., Albers, S. V., and Driessen, A. J. (2011). The sulfolobicin genes of Sulfolobus acidocaldarius encode novel antimicrobial proteins.J. Bacteriol. 193,4380-4387.
    • (2011) J. Bacteriol. , vol.193 , pp. 4380-4387
    • Ellen, A.F.1    Rohulya, O.V.2    Fusetti, E.3    Wagner, M.4    Albers, S.V.5    Driessen, A.J.6
  • 39
    • 35148873213 scopus 로고    scopus 로고
    • Are S-layers exoskeletons? The basic function of protein surface layers revisited
    • Engelhardt, H. (2007a). Are S-layers exoskeletons? The basic function of protein surface layers revisited. J. Struct Biol. 160, 115-124.
    • (2007) J. Struct Biol. , vol.160 , pp. 115-124
    • Engelhardt, H.1
  • 40
    • 35148893696 scopus 로고    scopus 로고
    • Mechanism of osmoprotection by archaeal S-layers: a theoretical study
    • Engelhardt, H. (2007b). Mechanism of osmoprotection by archaeal S-layers: a theoretical study. J. Struct. Biol. 160, 190-199.
    • (2007) J. Struct. Biol. , vol.160 , pp. 190-199
    • Engelhardt, H.1
  • 41
    • 25844454133 scopus 로고    scopus 로고
    • Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis
    • Falb, M., Pfeiffer, F., Palm, P., Rodewald, K., Hickmann, V., Tittor, J., and Oesterhelt, D. (2005). Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis. Genome Res. 15, 1336-1343.
    • (2005) Genome Res , vol.15 , pp. 1336-1343
    • Falb, M.1    Pfeiffer, F.2    Palm, P.3    Rodewald, K.4    Hickmann, V.5    Tittor, J.6    Oesterhelt, D.7
  • 42
    • 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., and Pugsley, A. P. (2007). Signal recognition particle-dependent inner membrane targeting of the PulG Pseudopilin component of a type II secretion system. J. Bacteriol. 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
  • 43
    • 0030010138 scopus 로고    scopus 로고
    • Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin
    • Frolow, F., Harel, M., Sussman, J. L., Mevarech, M., and Shoham, M. (1996). Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin. Nat. Struct. Biol. 3, 452-458.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 452-458
    • Frolow, F.1    Harel, M.2    Sussman, J.L.3    Mevarech, M.4    Shoham, M.5
  • 45
    • 79551473399 scopus 로고    scopus 로고
    • Assembly and function of the archaeal flagellum
    • Ghosh, A., and Albers, S. V. (2011). Assembly and function of the archaeal flagellum. Biochem. Soc. Trans. 39, 64-69.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 64-69
    • Ghosh, A.1    Albers, S.V.2
  • 46
    • 36549088956 scopus 로고    scopus 로고
    • Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins
    • Gimenez, M. I., Dilks, K., and Pohlschroder, M. (2007). Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins. Mol. Microbiol. 66, 1597-1606.
    • (2007) Mol. Microbiol. , vol.66 , pp. 1597-1606
    • Gimenez, M.I.1    Dilks, K.2    Pohlschroder, M.3
  • 49
    • 70349595267 scopus 로고    scopus 로고
    • Protein targeting by the signal recognition particle
    • Grudnik, P., Bange, G., and Sinning, I. (2009). Protein targeting by the signal recognition particle. Biol. Chem. 390,775-782.
    • (2009) Biol. Chem. , vol.390 , pp. 775-782
    • Grudnik, P.1    Bange, G.2    Sinning, I.3
  • 50
    • 84855870250 scopus 로고    scopus 로고
    • Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification
    • Haft, D. H., Payne, S. H., and Selengut, J. D. (2012). Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification. J. Bacteriol. 194,36-48.
    • (2012) J. Bacteriol. , vol.194 , pp. 36-48
    • Haft, D.H.1    Payne, S.H.2    Selengut, J.D.3
  • 52
    • 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.,and Albers, S. V. (2012). Influence of cell surface structures on crenarchaeal biofilm formation using a thermostable green fluorescent protein. Environ. Microbiol. 14, 779-793.
    • (2012) Environ. Microbiol. , vol.14 , pp. 779-793
    • Henche, A.L.1    Koerdt, A.2    Ghosh, A.3    and Albers, S.V.4
  • 53
    • 0031888811 scopus 로고    scopus 로고
    • Archaeal binding protein-dependent ABC transporter: molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis
    • Horlacher, R., Xavier, K. B., Santos, H., Diruggiero, J., Kossmann, M., and Boos, W (1998). Archaeal binding protein-dependent ABC transporter: molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 180, 680-689.
    • (1998) J. Bacteriol. , vol.180 , pp. 680-689
    • Horlacher, R.1    Xavier, K.B.2    Santos, H.3    Diruggiero, J.4    Kossmann, M.5    Boos, W.6
  • 54
    • 0037007636 scopus 로고    scopus 로고
    • A new phylum of archaea represented by a nano-sized hyperthermophilic symbiont
    • Huber, H., Hohn, M. J., Rachel, R., Fuchs, T., Wimmer, V. C., and Stetter, K. O. (2002). A new phylum of archaea represented by a nano-sized hyperthermophilic symbiont. Nature 417, 63-67.
    • (2002) Nature , vol.417 , pp. 63-67
    • Huber, H.1    Hohn, M.J.2    Rachel, R.3    Fuchs, T.4    Wimmer, V.C.5    Stetter, K.O.6
  • 55
    • 29244438994 scopus 로고    scopus 로고
    • Characterisation of a highly stable alpha-amylase from the halophilic archaeon Haloarcula hispanica
    • Hutcheon, G. W., Vasisht, N., and Bolhuis, A. (2005). Characterisation of a highly stable alpha-amylase from the halophilic archaeon Haloarcula hispanica. Extremophiles 9, 487-495.
    • (2005) Extremophiles , vol.9 , pp. 487-495
    • Hutcheon, G.W.1    Vasisht, N.2    Bolhuis, A.3
  • 56
    • 58149295961 scopus 로고    scopus 로고
    • Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em
    • Hutchings, M. I., Palmer, T., Harrington, D. J., and Sutcliffe, I. C. (2009). Lipoprotein biogenesis in Gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em. Trends Microbiol. 17, 13-21.
    • (2009) Trends Microbiol , vol.17 , pp. 13-21
    • Hutchings, M.I.1    Palmer, T.2    Harrington, D.J.3    Sutcliffe, I.C.4
  • 57
    • 83755174215 scopus 로고    scopus 로고
    • Identification of surprisingly diverse type IV pili, across a broad range of Gram-positive bacteria
    • doi:10.1371/journal.pone.0028919
    • Imam, S., Chen, Z., Roos, D. S., and Pohlschroder, M. (2011). Identification of surprisingly diverse type IV pili, across a broad range of Gram-positive bacteria. PLoS ONE 6, e28919. doi:10.1371/journal.pone.0028919
    • (2011) PLoS ONE , vol.6
    • Imam, S.1    Chen, Z.2    Roos, D.S.3    Pohlschroder, M.4
  • 58
    • 0038305947 scopus 로고    scopus 로고
    • Post-translational secretion of fusion proteins in the halophilic archaea Haloferax volcanii
    • Irihimovitch, V., and Eichler, J. (2003). Post-translational secretion of fusion proteins in the halophilic archaea Haloferax volcanii. J. Biol. Chem. 278, 12881-12887.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12881-12887
    • Irihimovitch, V.1    Eichler, J.2
  • 59
    • 79958134297 scopus 로고    scopus 로고
    • Biosynthesis and role of N-linked glycosylation in cell surface structures of archaea with a focus on flagella and s layers
    • Jarrell, K. F., Jones, G. M., and Nair, D. B. (2010). Biosynthesis and role of N-linked glycosylation in cell surface structures of archaea with a focus on flagella and s layers. Int. J. Microbiol. 2010,470138.
    • (2010) Int. J. Microbiol. , vol.2010 , pp. 470138
    • Jarrell, K.F.1    Jones, G.M.2    Nair, D.B.3
  • 60
    • 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., and Chong, J. P. (2011). Flagella and pili are both necessary for efficient attachment of Methanococcus maripaludis to surfaces. FEMS Microbiol. Lett. 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.4
  • 61
    • 18844453179 scopus 로고    scopus 로고
    • Type III secretion: a secretory pathway serving both motility and virulence (review)
    • Journet, L., Hughes, K. T., and Cornelis, G. R. (2005). Type III secretion: a secretory pathway serving both motility and virulence (review). Mol. Membr. Biol. 22, 41-50.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 41-50
    • Journet, L.1    Hughes, K.T.2    Cornelis, G.R.3
  • 63
    • 49749094746 scopus 로고    scopus 로고
    • Ignicoccus hospitalis and Nanoarchaeum equitans: ultrastructure, cell-cell interaction, and 3D reconstruction from serial sections of freeze-substituted cells and by electron cryotomography
    • Junglas, B., Briegel, A., Burghardt, T., Walther, P., Wirth, R., Huber, H., and Rachel, R. (2008). Ignicoccus hospitalis and Nanoarchaeum equitans: ultrastructure, cell-cell interaction, and 3D reconstruction from serial sections of freeze-substituted cells and by electron cryotomography. Arch. Microbiol. 190, 395-408.
    • (2008) Arch. Microbiol. , vol.190 , pp. 395-408
    • Junglas, B.1    Briegel, A.2    Burghardt, T.3    Walther, P.4    Wirth, R.5    Huber, H.6    Rachel, R.7
  • 64
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Kall, L., Krogh, A., and Sonnhammer, E. L. (2004). A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol. 338, 1027-1036.
    • (2004) J. Mol. Biol. , vol.338 , pp. 1027-1036
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 65
    • 0026541088 scopus 로고
    • Molecular cloning and sequencing of the gene for halophilic alkaline serine protease (halolysin) from an unidentified halophilic strain (172P1) and expression of the gene in Haloferax volcanii
    • Kamekura, M., Seno, Y., Holmes, M. L., and Dyallsmith, M. L. (1992). Molecular cloning and sequencing of the gene for halophilic alkaline serine protease (halolysin) from an unidentified halophilic strain (172P1) and expression of the gene in Haloferax volcanii. J. Bacteriol. 174,736-742.
    • (1992) J. Bacteriol. , vol.174 , pp. 736-742
    • Kamekura, M.1    Seno, Y.2    Holmes, M.L.3    Dyallsmith, M.L.4
  • 66
    • 0034767491 scopus 로고    scopus 로고
    • Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence
    • Kennedy, S. P., Ng, W V, Salzberg, S. L., Hood, L., and Dassarma, S. (2001). Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence. Genome Res. 11,1641-1650.
    • (2001) Genome Res , vol.11 , pp. 1641-1650
    • Kennedy, S.P.1    Ng, W.V.2    Salzberg, S.L.3    Hood, L.4    Dassarma, S.5
  • 67
    • 0033580929 scopus 로고    scopus 로고
    • Evidence for covalent attachment of diphytanylglyceryl phosphate to the cell-surface glycoprotein of Halobacterium halobium
    • Kikuchi, A., Sagami, H., and Ogura, K. (1999). Evidence for covalent attachment of diphytanylglyceryl phosphate to the cell-surface glycoprotein of Halobacterium halobium. J. Biol. Chem. 274,18011-18016.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18011-18016
    • Kikuchi, A.1    Sagami, H.2    Ogura, K.3
  • 68
    • 0027992184 scopus 로고
    • Cloning, expression, and nucleotide sequence of the α-amylase gene from the haloalkaliphilic archaeon Natronococcus sp. strain Ah-36
    • Kobayashi, T., Kanai, H., Aono, R., Horikoshi, K., and Kudo, T. (1994). Cloning, expression, and nucleotide sequence of the α-amylase gene from the haloalkaliphilic archaeon Natronococcus sp. strain Ah-36. J. Bacteriol. 176,5131-5134.
    • (1994) J. Bacteriol. , vol.176 , pp. 5131-5134
    • Kobayashi, T.1    Kanai, H.2    Aono, R.3    Horikoshi, K.4    Kudo, T.5
  • 69
    • 0037093395 scopus 로고    scopus 로고
    • A novel mode of sensory transduction in archaea: binding protein-mediated chemotaxis towards osmoprotectants and amino acids
    • Kokoeva, M. V., Storch, K. F., Klein, C., and Oesterhelt, D. (2002). A novel mode of sensory transduction in archaea: binding protein-mediated chemotaxis towards osmoprotectants and amino acids. EMBO J. 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
  • 70
    • 0037106458 scopus 로고    scopus 로고
    • Lipid modification of proteins in archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax vokanii follows protein translocation
    • Konrad, Z., and Eichler, J. (2002). Lipid modification of proteins in archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax vokanii follows protein translocation. Biochem. J. 366, 959-964.
    • (2002) Biochem. J. , vol.366 , pp. 959-964
    • Konrad, Z.1    Eichler, J.2
  • 71
    • 84866172198 scopus 로고    scopus 로고
    • Archaeal tetrathionate hydrolase goes viral: secretion of a sulfur metabolism enzyme in the form of virus-like particles
    • doi: 10.1128/AEM.01186-12. [Epub ahead of print]
    • Krupovic, M., Peixeiro, N., Bettstetter, M., Rachel, R., and Prangishvili, D. (2012). Archaeal tetrathionate hydrolase goes viral: secretion of a sulfur metabolism enzyme in the form of virus-like particles. Appl. Environ. Microbiol. doi: 10.1128/AEM.01186-12. [Epub ahead of print].
    • (2012) Appl. Environ. Microbiol.
    • Krupovic, M.1    Peixeiro, N.2    Bettstetter, M.3    Rachel, R.4    Prangishvili, D.5
  • 72
    • 77649265011 scopus 로고    scopus 로고
    • Energized outer membrane and spatial separation of metabolic processes in the hyperthermophilic archaeon Ignicoccus hospitalis
    • Kuper, U., Meyer, C., Muller, V., Rachel, R., and Huber, H. (2010). Energized outer membrane and spatial separation of metabolic processes in the hyperthermophilic archaeon Ignicoccus hospitalis. Proc. Natl. Acad. Sci. U.S.A. 107,3152-3156.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 3152-3156
    • Kuper, U.1    Meyer, C.2    Muller, V.3    Rachel, R.4    Huber, H.5
  • 73
    • 77953506268 scopus 로고    scopus 로고
    • Analysis of the twin-arginine motif of a haloarchaeal Tat substrate
    • Kwan,D., and Bolhuis, A. (2010). Analysis of the twin-arginine motif of a haloarchaeal Tat substrate. FEMS Microbiol. Lett. 308, 138-143.
    • (2010) FEMS Microbiol. Lett. , vol.308 , pp. 138-143
    • Kwan, D.1    Bolhuis, A.2
  • 76
    • 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., and Allers, T. (2011). Model organisms for genetics in the domain archaea: methanogens, halophiles, Thermococcales and Sulfolobales. FEMS Microbiol Rev. 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
  • 79
    • 0031857515 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a protein-serine/threonine phosphatase from the hyperthermophilic archaeon Pyrodictium abyssi TAG11
    • Mai, B., Frey, G., Swanson, R. V., Mathur, E. J., and Stetter, K. O. (1998). Molecular cloning and functional expression of a protein-serine/threonine phosphatase from the hyperthermophilic archaeon Pyrodictium abyssi TAG11. J. Bacteriol. 180,4030-4035.
    • (1998) J. Bacteriol. , vol.180 , pp. 4030-4035
    • Mai, B.1    Frey, G.2    Swanson, R.V.3    Mathur, E.J.4    Stetter, K.O.5
  • 80
    • 0028246909 scopus 로고
    • The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation
    • Mattar, S., Scharf, B., Kent, S. B., Rodewald, K., Oesterhelt, D., and Engelhard, M. (1994). The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation. J. Biol Chem. 269, 14939-14945.
    • (1994) J. Biol Chem. , vol.269 , pp. 14939-14945
    • Mattar, S.1    Scharf, B.2    Kent, S.B.3    Rodewald, K.4    Oesterhelt, D.5    Engelhard, M.6
  • 81
    • 0030156252 scopus 로고    scopus 로고
    • A hyperthermostable protease of the subtilisin family bound to the surface layer of the Archaeon Staphylothermus marinus
    • Mayr, J., Lupas, A., Kellermann, J., Eckerskorn, C., Baumeister, W., and Peters, J. (1996). A hyperthermostable protease of the subtilisin family bound to the surface layer of the Archaeon Staphylothermus marinus. Curr. Biol. 6, 739-749.
    • (1996) Curr. Biol. , vol.6 , pp. 739-749
    • Mayr, J.1    Lupas, A.2    Kellermann, J.3    Eckerskorn, C.4    Baumeister, W.5    Peters, J.6
  • 83
    • 0016123083 scopus 로고
    • Protein and carbohydrate composition of the cell envelope of Halobacterium salinarium
    • Mescher, M. F., Strominger, J. L., and Watson, S. W. (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
  • 85
    • 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., and Huber, R. (2005). The unique structure of archaeal "hami," highly complex cell appendages with nano-grappling hooks. Mol Microbiol. 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
  • 89
    • 75749143418 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the early stage of protein translocation through the Sec translocon
    • Mori, T., Ishitani, R., Tsukazaki, T., Nureki, O., and Sugita, Y. (2010). Molecular mechanisms underlying the early stage of protein translocation through the Sec translocon. Biochemistry 49, 945-950.
    • (2010) Biochemistry , vol.49 , pp. 945-950
    • Mori, T.1    Ishitani, R.2    Tsukazaki, T.3    Nureki, O.4    Sugita, Y.5
  • 91
    • 50049087513 scopus 로고    scopus 로고
    • Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane -distinct translocases and mechanisms
    • Natale, P., Bruser, T., and Driessen, A. J. (2008). Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane -distinct translocases and mechanisms. Biochim. Biophys. Acta 1778, 1735-1756.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1735-1756
    • Natale, P.1    Bruser, T.2    Driessen, A.J.3
  • 92
    • 2342652283 scopus 로고    scopus 로고
    • The outer membrane of the hyperthermophilic archaeon Ignicoccus: dynamics, ultrastructure and composition
    • Nather, D. J., and Rachel, R. (2004). The outer membrane of the hyperthermophilic archaeon Ignicoccus: dynamics, ultrastructure and composition. Biochem. Soc. Trans. 32, 199-203.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 199-203
    • Nather, D.J.1    Rachel, R.2
  • 93
    • 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., and Wirth, R. (2006). Flagella of Pyrococcus furiosus: multifunctional organelles, made for swimming, adhesion to various surfaces, and cell-cell contacts. J. Bacteriol. 188, 6915-6923.
    • (2006) J. Bacteriol. , vol.188 , pp. 6915-6923
    • Nather, D.J.1    Rachel, R.2    Wanner, G.3    Wirth, R.4
  • 95
    • 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., and Jarrell, K. F. (2009). Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD. J. Bacteriol. 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
  • 97
    • 0036165760 scopus 로고    scopus 로고
    • Halocins and sulfolobicins: the emerging story of archaeal protein and peptide antibiotics
    • O'Connor, E. M., and Shand, R. F. (2002). Halocins and sulfolobicins: the emerging story of archaeal protein and peptide antibiotics. J. Ind. Microbiol Biotechnol. 28, 23-31.
    • (2002) J. Ind. Microbiol Biotechnol. , vol.28 , pp. 23-31
    • O'Connor, E.M.1    Shand, R.F.2
  • 98
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • Okuda, S., and Tokuda, H. (2011). Lipoprotein sorting in bacteria. Annu. Rev. Microbiol. 65,239-259.
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 239-259
    • Okuda, S.1    Tokuda, H.2
  • 99
    • 0034725568 scopus 로고    scopus 로고
    • Evidence for post-translational membrane insertion of the integral membrane protein bacterioopsin expressed in the heterologous halophilic archaeon Haloferax volcanii
    • Ortenberg, R., and Mevarech, M. (2000). Evidence for post-translational membrane insertion of the integral membrane protein bacterioopsin expressed in the heterologous halophilic archaeon Haloferax volcanii. J. Biol Chem. 275,22839-22846.
    • (2000) J. Biol Chem. , vol.275 , pp. 22839-22846
    • Ortenberg, R.1    Mevarech, M.2
  • 101
    • 78249283543 scopus 로고    scopus 로고
    • The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with chitobiose-linked N-glycans
    • PMID: 20936123
    • Peyfoon, E., Meyer, B., Hitchen, P. G., Panico, M., Morris, H. R., Haslam, S. M., Albers, S. V., and Dell, A. (2010). The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with chitobiose-linked N-glycans. Archaea. PMID: 20936123.
    • (2010) Archaea
    • Peyfoon, E.1    Meyer, B.2    Hitchen, P.G.3    Panico, M.4    Morris, H.R.5    Haslam, S.M.6    Albers, S.V.7    Dell, A.8
  • 102
    • 79958816876 scopus 로고    scopus 로고
    • Archaeal type IV pilus-like structures - evolutionarily conserved prokaryotic surface organelles
    • Pohlschroder, M., Ghosh, A., Tripepi, M., and Albers, S.V (2011). Archaeal type IV pilus-like structures - evolutionarily conserved prokaryotic surface organelles. Curr. Opin. Microbiol. 14, 357-363.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 357-363
    • Pohlschroder, M.1    Ghosh, A.2    Tripepi, M.3    Albers, S.V.4
  • 103
    • 27844495651 scopus 로고    scopus 로고
    • Protein transport in archaea: Sec and twin arginine translocation pathways
    • Pohlschroder, M., Gimenez, M. I., and Jarrell, K. F. (2005a). Protein transport in archaea: Sec and twin arginine translocation pathways. Curr. Opin. Microbiol. 8, 713-719.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 713-719
    • Pohlschroder, M.1    Gimenez, M.I.2    Jarrell, K.F.3
  • 105
    • 0034069304 scopus 로고    scopus 로고
    • Sulfolobicins, specific proteinaceous toxins produced by strains of the extremely thermophilic archaeal genus Sulfolobus
    • Prangishvili, D., Holz, I., Stieger, E., Nickell, S., Kristjansson, J. K., and Zillig, W (2000). Sulfolobicins, specific proteinaceous toxins produced by strains of the extremely thermophilic archaeal genus Sulfolobus. J. Bacteriol. 182,2985-2988.
    • (2000) J. Bacteriol. , vol.182 , pp. 2985-2988
    • Prangishvili, D.1    Holz, I.2    Stieger, E.3    Nickell, S.4    Kristjansson, J.K.5    Zillig, W.6
  • 106
    • 0033883369 scopus 로고    scopus 로고
    • Halocin S8: a 36-amino-acid microhalocin from the haloarchaeal strain S8a
    • Price, L. B., and Shand, R. F. (2000). Halocin S8: a 36-amino-acid microhalocin from the haloarchaeal strain S8a.J. Bacteriol. 182,4951-4958.
    • (2000) J. Bacteriol. , vol.182 , pp. 4951-4958
    • Price, L.B.1    Shand, R.F.2
  • 107
    • 84872599788 scopus 로고    scopus 로고
    • An extracellular tetrathionate hydrolase from the thermoacidophilic archaeon Acidianus ambivalens with an activity optimum at pH 1
    • doi:10.3389/fmicb.2011.00068
    • Protze, J., Muller, F., Lauber, K., Nass, B., Mentele, R., Lottspeich, F., and Kletzin, A. (2011). An extracellular tetrathionate hydrolase from the thermoacidophilic archaeon Acidianus ambivalens with an activity optimum at pH 1. Front. Microbiol. 2:68. doi:10.3389/fmicb.2011.00068
    • (2011) Front. Microbiol. , vol.2 , pp. 68
    • Protze, J.1    Muller, F.2    Lauber, K.3    Nass, B.4    Mentele, R.5    Lottspeich, F.6    Kletzin, A.7
  • 110
    • 79851514906 scopus 로고    scopus 로고
    • Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria
    • Robinson, C., Matos, C. F., Beck, D., Ren, C., Lawrence, J., Vasisht, N., and Mendel, S. (2011). Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria. Biochim. Biophys. Acta 1808, 876-884.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 876-884
    • Robinson, C.1    Matos, C.F.2    Beck, D.3    Ren, C.4    Lawrence, J.5    Vasisht, N.6    Mendel, S.7
  • 111
    • 0036038940 scopus 로고    scopus 로고
    • Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway
    • Rose, R. W., Bruser, T., Kissinger, J. C., and Pohlschroder, M. (2002). Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway. Mol. Microbiol. 45,943-950.
    • (2002) Mol. Microbiol. , vol.45 , pp. 943-950
    • Rose, R.W.1    Bruser, T.2    Kissinger, J.C.3    Pohlschroder, M.4
  • 112
    • 0035347175 scopus 로고    scopus 로고
    • Natural communities of novel archaea and bacteria growing in cold sulfurous springs with a string-of-pearls-like morphology
    • Rudolph, C., Wanner, G., and Huber, R. (2001). Natural communities of novel archaea and bacteria growing in cold sulfurous springs with a string-of-pearls-like morphology. Appl. Environ. Microbiol. 67, 2336-2344.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2336-2344
    • Rudolph, C.1    Wanner, G.2    Huber, R.3
  • 113
    • 79959304018 scopus 로고    scopus 로고
    • Cell cycles and cell division in the archaea
    • Samson, R. Y., and Bell, S. D. (2011). Cell cycles and cell division in the archaea. Curr. Opin. Microbiol. 14, 350-356.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 350-356
    • Samson, R.Y.1    Bell, S.D.2
  • 114
    • 58149230938 scopus 로고    scopus 로고
    • A role for the ESCRT system in cell division in archaea
    • Samson, R. Y., Obita, T., Freund, S. M., Williams, R. L., and Bell, S. D. (2008). A role for the ESCRT system in cell division in archaea. Science 322,1710-1713.
    • (2008) Science , vol.322 , pp. 1710-1713
    • Samson, R.Y.1    Obita, T.2    Freund, S.M.3    Williams, R.L.4    Bell, S.D.5
  • 115
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran, K., and Wu, H. C. (1994). Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269, 19701-19706.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 116
    • 33748333118 scopus 로고    scopus 로고
    • Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii
    • Saunders, N. F. W., Ng, C., Raftery, M., Guilhaus, M., Goodchild, A., and Cavicchioli, R. (2006). Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii. J. Proteome Res. 5, 2457-2464.
    • (2006) J. Proteome Res. , vol.5 , pp. 2457-2464
    • Saunders, N.F.W.1    Ng, C.2    Raftery, M.3    Guilhaus, M.4    Goodchild, A.5    Cavicchioli, R.6
  • 117
    • 33751107167 scopus 로고    scopus 로고
    • An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp J7: gene cloning, expression and characterization
    • Shi, W. L., Tang, X. F., Huang, Y. P., Gan, F., Tang, B., and Shen, P. (2006). An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp J7: gene cloning, expression and characterization. Extremophiles 10, 599-606.
    • (2006) Extremophiles , vol.10 , pp. 599-606
    • Shi, W.L.1    Tang, X.F.2    Huang, Y.P.3    Gan, F.4    Tang, B.5    Shen, P.6
  • 118
    • 79551497485 scopus 로고    scopus 로고
    • Potential role of cellular ESCRT proteins in the STIV life cycle
    • Snyder, J. C., and Young, M. J. (2011). Potential role of cellular ESCRT proteins in the STIV life cycle. Biochem. Soc. Trans. 39, 107-110.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 107-110
    • Snyder, J.C.1    Young, M.J.2
  • 119
    • 49149096271 scopus 로고    scopus 로고
    • Virus-like vesicles and extracellular DNA produced by hyperthermophilic archaea of the order Thermococcales
    • Soler, N., Marguet, E., Verbavatz, J. M., and Forterre, P. (2008). Virus-like vesicles and extracellular DNA produced by hyperthermophilic archaea of the order Thermococcales. Res. Microbiol. 159, 390-399.
    • (2008) Res. Microbiol. , vol.159 , pp. 390-399
    • Soler, N.1    Marguet, E.2    Verbavatz, J.M.3    Forterre, P.4
  • 120
    • 82155168216 scopus 로고    scopus 로고
    • Sortase enzymes in Gram-positive bacteria
    • Spirig, T., Weiner, E. M., and Clubb, R. T. (2011). Sortase enzymes in Gram-positive bacteria. Mol. Microbiol. 82, 1044-1059.
    • (2011) Mol. Microbiol. , vol.82 , pp. 1044-1059
    • Spirig, T.1    Weiner, E.M.2    Clubb, R.T.3
  • 121
    • 77957835036 scopus 로고    scopus 로고
    • Mutational and bioinformatic analysis of haloarchaeal lipobox-containing proteins
    • Storf, S., Pfeiffer, F., Dilks, K., Chen, Z. Q., Imam, S., and Pohlschroder, M. (2010). Mutational and bioinformatic analysis of haloarchaeal lipobox-containing proteins. Archaea 2010,11.
    • (2010) Archaea , vol.2010 , pp. 11
    • Storf, S.1    Pfeiffer, F.2    Dilks, K.3    Chen, Z.Q.4    Imam, S.5    Pohlschroder, M.6
  • 122
    • 79955705583 scopus 로고    scopus 로고
    • Morphological and structural aspects of the extremely halophilic archaeon Haloquadratum walsbyi
    • doi:10.1371/journal.pone.0018653
    • Sublimi Saponetti, M., Bobba, F., Salerno, G., Scarfato, A., Corcelli, A., and Cucolo, A. (2011). Morphological and structural aspects of the extremely halophilic archaeon Haloquadratum walsbyi. PLoS ONE 6, e18653. doi:10.1371/journal.pone.0018653
    • (2011) PLoS ONE , vol.6
    • Sublimi Saponetti, M.1    Bobba, F.2    Salerno, G.3    Scarfato, A.4    Corcelli, A.5    Cucolo, A.6
  • 123
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper, M., Berg, E., Mengele, R., and Strobel, I. (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
  • 124
    • 22144485200 scopus 로고    scopus 로고
    • A single gene directs both production and immunity of halocin C8 in a haloarchaeal strain AS7092
    • Sun, C., Li, Y., Mei, S., Lu, Q., Zhou, L., and Xiang, H. (2005). A single gene directs both production and immunity of halocin C8 in a haloarchaeal strain AS7092. Mol. Microbiol. 57, 537-549.
    • (2005) Mol. Microbiol. , vol.57 , pp. 537-549
    • Sun, C.1    Li, Y.2    Mei, S.3    Lu, Q.4    Zhou, L.5    Xiang, H.6
  • 126
    • 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., and Pohlschroder, M. (2007b). 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
    • Szabo, Z.1    Stahl, A.O.2    Albers, S.V.3    Kissinger, J.C.4    Driessen, A.J.5    Pohlschroder, M.6
  • 127
    • 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., and Wirth, R. (2008). The Mth60 fimbriae of Methanothermobacter thermoautotrophicus are functional adhesins. Environ. Microbiol. 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
  • 128
    • 77955372826 scopus 로고    scopus 로고
    • Investigating lipoprotein biogenesis and function in the model Gram-positive bacterium Streptomyces coelicolor
    • Thompson, B. J., Widdick, D. A., Hicks, M. G., Chandra, G., Sutcliffe, I. C., Palmer, T., and Hutchings, M. I. (2010). Investigating lipoprotein biogenesis and function in the model Gram-positive bacterium Streptomyces coelicolor. Mol. Microbiol. 77, 943-957.
    • (2010) Mol. Microbiol. , vol.77 , pp. 943-957
    • Thompson, B.J.1    Widdick, D.A.2    Hicks, M.G.3    Chandra, G.4    Sutcliffe, I.C.5    Palmer, T.6    Hutchings, M.I.7
  • 129
    • 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., and Pohlschroder, M. (2010). Haloferax volcanii flagella are required for motility but are not involved in PibD-dependent surface adhesion. J. Bacteriol. 192, 3093-3102.
    • (2010) J. Bacteriol. , vol.192 , pp. 3093-3102
    • Tripepi, M.1    Imam, S.2    Pohlschroder, M.3
  • 130
    • 27244446613 scopus 로고    scopus 로고
    • Type I signal peptidase: an overview
    • Tuteja, R. (2005). Type I signal peptidase: an overview. Arch. Biochem. Biophys. 441, 107-111.
    • (2005) Arch. Biochem. Biophys. , vol.441 , pp. 107-111
    • Tuteja, R.1
  • 131
    • 75749150899 scopus 로고    scopus 로고
    • LccA, an archaeal laccase secreted as a highly stable glycoprotein into the extracellular medium by Haloferax volcanii
    • Uthandi, S., Saad, B., Humbard, M. A., and Maupin-Furlow, J. A. (2010). LccA, an archaeal laccase secreted as a highly stable glycoprotein into the extracellular medium by Haloferax volcanii. Appl. Environ. Microbiol. 76, 733-743.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 733-743
    • Uthandi, S.1    Saad, B.2    Humbard, M.A.3    Maupin-Furlow, J.A.4
  • 133
    • 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., and Jarrell, K. E (2008). Identification of a putative acetyltransferase gene, MMP0350, which affects proper assembly of both flagella and pili in the archaeon Methanococcus maripaludis. J. Bacteriol. 190, 5300-5307.
    • (2008) J. Bacteriol. , vol.190 , pp. 5300-5307
    • Van Dyke, D.J.1    Wu, J.2    Ng, S.Y.3    Kanbe, M.4    Chaban, B.5    Aizawa, S.6    Jarrell, K.E.7
  • 135
  • 136
    • 76149128021 scopus 로고    scopus 로고
    • Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part II: the effect of different methylated growth substrates
    • Williams, T. J., Burg, D. W., Ertan, H., Raftery, M. J., Poljak, A., Guilhaus, M., and Cavicchioli, R. (2010a). Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part II: the effect of different methylated growth substrates. J. Proteome Res. 9, 653-663.
    • (2010) J. Proteome Res. , vol.9 , pp. 653-663
    • Williams, T.J.1    Burg, D.W.2    Ertan, H.3    Raftery, M.J.4    Poljak, A.5    Guilhaus, M.6    Cavicchioli, R.7
  • 137
    • 76149124222 scopus 로고    scopus 로고
    • Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part I: the effect of growth temperature
    • Williams, T. J., Burg, D. W., Raftery, M. J., Poljak, A., Guilhaus, M., Pilak, O., and Cavicchioli, R. (2010b). Global proteomic analysis of the insoluble, soluble, and supernatant fractions of the psychrophilic archaeon Methanococcoides burtonii. Part I: the effect of growth temperature. J. Proteome Res. 9, 640-652.
    • (2010) J. Proteome Res. , vol.9 , pp. 640-652
    • Williams, T.J.1    Burg, D.W.2    Raftery, M.J.3    Poljak, A.4    Guilhaus, M.5    Pilak, O.6    Cavicchioli, R.7
  • 138
    • 0037226536 scopus 로고    scopus 로고
    • Targeted disruption of the alpha-amylase gene in the hyperthermophilic archaeon Sulfolobus solfataficus
    • Worthington, P., Hoang, V., Perez-Pomares, F., and Blum, P. (2003). Targeted disruption of the alpha-amylase gene in the hyperthermophilic archaeon Sulfolobus solfataficus. J. Bacteriol. 185, 482-488.
    • (2003) J. Bacteriol. , vol.185 , pp. 482-488
    • Worthington, P.1    Hoang, V.2    Perez-Pomares, F.3    Blum, P.4
  • 139
    • 80051830597 scopus 로고    scopus 로고
    • Functional insight into the C-terminal extension of halolysin SptA from haloarchaeon Natrinema sp J7
    • doi:10.1371/journal.pone.0023562
    • Xu, Z., Du, X., Li, T., Gan, F., Tang, B., and Tang, X.-F. (2011). Functional insight into the C-terminal extension of halolysin SptA from haloarchaeon Natrinema sp J7. PLoS ONE 6, e23562. doi:10.1371/journal.pone.0023562
    • (2011) PLoS ONE , vol.6
    • Xu, Z.1    Du, X.2    Li, T.3    Gan, F.4    Tang, B.5    Tang, X.-F.6
  • 140
    • 73849092886 scopus 로고    scopus 로고
    • Protein transport across and into cell membranes in bacteria and archaea
    • Yuan, J., Zweers, J. C., Van Dijl, J. M., and Dalbey, R. E. (2010). Protein transport across and into cell membranes in bacteria and archaea. Cell. Mol. Life Sci. 67, 179-199.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 179-199
    • Yuan, J.1    Zweers, J.C.2    Van Dijl, J.M.3    Dalbey, R.E.4
  • 143
    • 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., and Albers, S. V. (2007). Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus. Mol. Microbiol. 64, 795-806.
    • (2007) Mol. Microbiol. , vol.64 , pp. 795-806
    • Zolghadr, B.1    Weber, S.2    Szabo, Z.3    Driessen, A.J.4    Albers, S.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.