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Volumn 3, Issue 3, 2012, Pages 163-170

A phylum level analysis reveals lipoprotein biosynthesis to be a fundamental property of bacteria

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ACYLTRANSFERASE LNT; BACTERIAL ENZYME; BACTERIAL PROTEIN; BACTERIUM LIPOPROTEIN; DIACYLGLYCEROL TRANSFERASE; SIGNAL PEPTIDASE; SIGNAL PEPTIDASE LSP; UNCLASSIFIED DRUG;

EID: 84862901721     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-012-2023-8     Document Type: Article
Times cited : (39)

References (69)
  • 2
    • 33645972887 scopus 로고    scopus 로고
    • A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins
    • Babu, M. M., Priya, M. L., Selvan, A. T., Madera, M., Gough, J., Aravind, L., and Sankaran, K. (2006). A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins. J Bacteriol 188, 2761-2773.
    • (2006) J Bacteriol , vol.188 , pp. 2761-2773
    • Babu, M.M.1    Priya, M.L.2    Selvan, A.T.3    Madera, M.4    Gough, J.5    Aravind, L.6    Sankaran, K.7
  • 3
    • 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
  • 4
    • 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
  • 6
    • 77956860575 scopus 로고
    • Lipoproteins: structure function, biosynthesis and model for protein export
    • Braun, V., and Wu, H. C. (1994). Lipoproteins: structure function, biosynthesis and model for protein export. New Comp. Biochem. 27, 319-341.
    • (1994) New Comp. Biochem. , vol.27 , pp. 319-341
    • Braun, V.1    Wu, H.C.2
  • 7
    • 33748783783 scopus 로고    scopus 로고
    • Host defenses against Staphylococcus aureus infection require recognition of bacterial lipoproteins
    • Bubeck Wardenburg, J., Williams, W. A., and Missiakas, D. (2006). Host defenses against Staphylococcus aureus infection require recognition of bacterial lipoproteins. Proc Natl Acad Sci U S A 103, 13831-13836.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 13831-13836
    • Bubeck Wardenburg, J.1    Williams, W.A.2    Missiakas, D.3
  • 8
    • 75349096668 scopus 로고    scopus 로고
    • The essential Escherichia coli apolipoprotein N-acyltransferase (Lnt) exists as an extracytoplasmic thioester acyl-enzyme intermediate
    • Buddelmeijer, N., and Young, R. (2010). The essential Escherichia coli apolipoprotein N-acyltransferase (Lnt) exists as an extracytoplasmic thioester acyl-enzyme intermediate. Biochemistry 49, 341-346.
    • (2010) Biochemistry , vol.49 , pp. 341-346
    • Buddelmeijer, N.1    Young, R.2
  • 9
    • 37549029235 scopus 로고    scopus 로고
    • Mechanism and hydrophobic forces driving membrane protein insertion of subunit II of cytochrome bo3 oxidase
    • Celebi, N., Dalbey, R. E., and Yuan, J. (2008). Mechanism and hydrophobic forces driving membrane protein insertion of subunit II of cytochrome bo3 oxidase. J Mol Biol 375, 1282-1292.
    • (2008) J Mol Biol , vol.375 , pp. 1282-1292
    • Celebi, N.1    Dalbey, R.E.2    Yuan, J.3
  • 10
    • 4544272190 scopus 로고    scopus 로고
    • Enterococcal peptide sex pheromones: synthesis and control of biological activity
    • Chandler, J. R., and Dunny, G. M. (2004). Enterococcal peptide sex pheromones: synthesis and control of biological activity. Peptides 25, 1377-1388.
    • (2004) Peptides , vol.25 , pp. 1377-1388
    • Chandler, J.R.1    Dunny, G.M.2
  • 11
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley, D. O., Rapp, M., Granseth, E., Melén, K., Drew, D., and von Heijne, G. (2005). Global topology analysis of the Escherichia coli inner membrane proteome. Science 308, 1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melén, K.4    Drew, D.5    von Heijne, G.6
  • 12
    • 46049119823 scopus 로고    scopus 로고
    • Lipoprotein signal peptides are processed by Lsp and Eep of Streptococcus uberis
    • Denham, E. L., Ward, P. N., and Leigh, J. A. (2008). Lipoprotein signal peptides are processed by Lsp and Eep of Streptococcus uberis. J Bacteriol 190, 4641-4647.
    • (2008) J Bacteriol , vol.190 , pp. 4641-4647
    • Denham, E.L.1    Ward, P.N.2    Leigh, J.A.3
  • 14
    • 0037044719 scopus 로고    scopus 로고
    • Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals
    • Fukuda, A., Matsuyama, S., Hara, T., Nakayama, J., Nagasawa, H., and Tokuda, H. (2002). Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals. J Biol Chem 277, 43512-43518.
    • (2002) J Biol Chem , vol.277 , pp. 43512-43518
    • Fukuda, A.1    Matsuyama, S.2    Hara, T.3    Nakayama, J.4    Nagasawa, H.5    Tokuda, H.6
  • 15
    • 36549088956 scopus 로고    scopus 로고
    • Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins
    • Giménez, M. I., Dilks, K., and Pohlschröder, 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
    • Giménez, M.I.1    Dilks, K.2    Pohlschröder, M.3
  • 16
    • 0026111879 scopus 로고
    • Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli
    • Gupta, S. D., and Wu, H. C. (1991). Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli. FEMS Microbiol Lett 62, 37-41.
    • (1991) FEMS Microbiol Lett , vol.62 , pp. 37-41
    • Gupta, S.D.1    Wu, H.C.2
  • 18
    • 80051503015 scopus 로고    scopus 로고
    • Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase
    • Hillmann, F., Argentini, M., and Buddelmeijer, N. (2011). Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase. J Biol Chem 286, 27936-27946.
    • (2011) J Biol Chem , vol.286 , pp. 27936-27946
    • Hillmann, F.1    Argentini, M.2    Buddelmeijer, N.3
  • 20
    • 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
  • 21
    • 33947358982 scopus 로고    scopus 로고
    • A new screening method to identify inhibitors of the Lol (localization of lipoproteins) system, a novel antibacterial target
    • Ito, H., Ura, A., Oyamada, Y., Yoshida, H., Yamagishi, J., Narita, S., Matsuyama, S., and Tokuda, H. (2007). A new screening method to identify inhibitors of the Lol (localization of lipoproteins) system, a novel antibacterial target. Microbiol Immunol 51, 263-270.
    • (2007) Microbiol Immunol , vol.51 , pp. 263-270
    • Ito, H.1    Ura, A.2    Oyamada, Y.3    Yoshida, H.4    Yamagishi, J.5    Narita, S.6    Matsuyama, S.7    Tokuda, H.8
  • 22
    • 77957768681 scopus 로고    scopus 로고
    • Lipoprotein biosynthesis as a target for anti-Wolbachia treatment of filarial nematodes
    • Johnston, K. L., Wu, B., Guimarães, A., Ford, L., Slatko, B. E., and Taylor, M. J. (2010). Lipoprotein biosynthesis as a target for anti-Wolbachia treatment of filarial nematodes. Parasit Vectors 3, 99.
    • (2010) Parasit Vectors , vol.3 , pp. 99
    • Johnston, K.L.1    Wu, B.2    Guimarães, A.3    Ford, L.4    Slatko, B.E.5    Taylor, M.J.6
  • 25
  • 26
    • 79958125256 scopus 로고    scopus 로고
    • Surface localization determinants of Borrelia OspC/Vsp family lipoproteins
    • Kumru, O. S., Schulze, R. J., Rodnin, M. V., Ladokhin, A. S., and Zückert, W. R. (2011). Surface localization determinants of Borrelia OspC/Vsp family lipoproteins. J Bacteriol 193, 2814-2825.
    • (2011) J Bacteriol , vol.193 , pp. 2814-2825
    • Kumru, O.S.1    Schulze, R.J.2    Rodnin, M.V.3    Ladokhin, A.S.4    Zückert, W.R.5
  • 27
    • 0036452117 scopus 로고    scopus 로고
    • Purification and characterization of the major lipoprotein (P28) of Spiroplasma apis
    • Le Hénaff, M., Crémet, J. Y., and Fontenelle, C. (2002). Purification and characterization of the major lipoprotein (P28) of Spiroplasma apis. Protein Expr Purif 24, 489-496.
    • (2002) Protein Expr Purif , vol.24 , pp. 489-496
    • Le Hénaff, M.1    Crémet, J.Y.2    Fontenelle, C.3
  • 28
    • 51549111175 scopus 로고    scopus 로고
    • Novel inner membrane retention signals in Pseudomonas aeruginosa lipoproteins
    • Lewenza, S., Mhlanga, M. M., and Pugsley, A. P. (2008). Novel inner membrane retention signals in Pseudomonas aeruginosa lipoproteins. J Bacteriol 190, 6119-6125.
    • (2008) J Bacteriol , vol.190 , pp. 6119-6125
    • Lewenza, S.1    Mhlanga, M.M.2    Pugsley, A.P.3
  • 29
    • 33646575276 scopus 로고    scopus 로고
    • Direct visualization of red fluorescent lipoproteins indicates conservation of the membrane sorting rules in the family Enterobacteriaceae
    • Lewenza, S., Vidal-Ingigliardi, D., and Pugsley, A. P. (2006). Direct visualization of red fluorescent lipoproteins indicates conservation of the membrane sorting rules in the family Enterobacteriaceae. J Bacteriol 188, 3516-3524.
    • (2006) J Bacteriol , vol.188 , pp. 3516-3524
    • Lewenza, S.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 30
    • 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. H., 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.H.3    Rodewald, K.4    Oesterhelt, D.5    Engelhard, M.6
  • 31
    • 79959539151 scopus 로고    scopus 로고
    • ABC transporters involved in the biogenesis of the outer membrane in gram-negative bacteria
    • Narita, S.-I. (2011). ABC transporters involved in the biogenesis of the outer membrane in gram-negative bacteria. Biosci Biotechnol Biochem 75, 1044-1054.
    • (2011) Biosci Biotechnol Biochem , vol.75 , pp. 1044-1054
    • Narita, S.-I.1
  • 32
    • 31844431988 scopus 로고    scopus 로고
    • An ABC transporter mediating the membrane detachment of bacterial lipoproteins depending on their sorting signals
    • Narita, S.-I., and Tokuda, H. (2006). An ABC transporter mediating the membrane detachment of bacterial lipoproteins depending on their sorting signals. FEBS Lett 580, 1164-1170.
    • (2006) FEBS Lett , vol.580 , pp. 1164-1170
    • Narita, S.-I.1    Tokuda, H.2
  • 33
    • 34250351484 scopus 로고    scopus 로고
    • Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins
    • Narita, S.-I., and Tokuda, H. (2007). Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins. J Biol Chem 282, 13372-13378.
    • (2007) J Biol Chem , vol.282 , pp. 13372-13378
    • Narita, S.-I.1    Tokuda, H.2
  • 34
    • 80052551712 scopus 로고    scopus 로고
    • Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase
    • Narita, S.-I., and Tokuda, H. (2011). Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase. J Bacteriol 193, 4832-4840.
    • (2011) J Bacteriol , vol.193 , pp. 4832-4840
    • Narita, S.-I.1    Tokuda, H.2
  • 35
    • 42049092254 scopus 로고    scopus 로고
    • Chromatophore genome sequence of Paulinella sheds light on acquisition of photosynthesis by eukaryotes
    • Nowack, E. C. M., Melkonian, M., and Glöckner, G. (2008). Chromatophore genome sequence of Paulinella sheds light on acquisition of photosynthesis by eukaryotes. Curr Biol 18, 410-418.
    • (2008) Curr Biol , vol.18 , pp. 410-418
    • Nowack, E.C.M.1    Melkonian, M.2    Glöckner, G.3
  • 36
    • 65249085615 scopus 로고    scopus 로고
    • Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB
    • Okuda, S., and Tokuda, H. (2009). Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB. Proc Natl Acad Sci U S A 106, 5877-5882.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5877-5882
    • Okuda, S.1    Tokuda, H.2
  • 37
    • 84861220038 scopus 로고    scopus 로고
    • Phosphatidylglycerol: prolipoprotein diacylglyceryl transferase (Lgt) of E. coli has seven transmembrane segments and its essential residues are embedded in the membrane
    • doi: 10. 1128/JB. 06641-11
    • Pailler, J., Aucher, W., Pires, M., and Buddelmeijer, N. (2012). Phosphatidylglycerol: prolipoprotein diacylglyceryl transferase (Lgt) of E. coli has seven transmembrane segments and its essential residues are embedded in the membrane. J Bacteriol. doi: 10. 1128/JB. 06641-11.
    • (2012) J Bacteriolo
    • Pailler, J.1    Aucher, W.2    Pires, M.3    Buddelmeijer, N.4
  • 39
    • 0028817888 scopus 로고
    • Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions
    • Qi, H.-Y., Sankaran, K., Gan, K., and Wu, H. C. (1995). Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions. J Bacteriol 177, 6820-6824.
    • (1995) J Bacteriol , vol.177 , pp. 6820-6824
    • Qi, H.-Y.1    Sankaran, K.2    Gan, K.3    Wu, H.C.4
  • 40
    • 52449085554 scopus 로고    scopus 로고
    • Methods for the bioinformatic identification of bacterial lipoproteins encoded in the genomes of Gram-positive bacteria
    • Rahman, O., Cummings, S. P., Harrington, D. J., and Sutcliffe, I. C. (2008). Methods for the bioinformatic identification of bacterial lipoproteins encoded in the genomes of Gram-positive bacteria. World J Microbiol Biotechnol 24, 2377-2382.
    • (2008) World J Microbiol Biotechnol , vol.24 , pp. 2377-2382
    • Rahman, O.1    Cummings, S.P.2    Harrington, D.J.3    Sutcliffe, I.C.4
  • 41
    • 80155150932 scopus 로고    scopus 로고
    • Lipoproteins of Enterococcus faecalis: bioinformatic identification, expression analysis and relation to virulence
    • Reffuveille, F., Leneveu, C., Chevalier, S., Auffray, Y., and Rincé, A. (2011). Lipoproteins of Enterococcus faecalis: bioinformatic identification, expression analysis and relation to virulence. Microbiology 157, 3001-3013.
    • (2011) Microbiology , vol.157 , pp. 3001-3013
    • Reffuveille, F.1    Leneveu, C.2    Chevalier, S.3    Auffray, Y.4    Rincé, A.5
  • 42
    • 1542782546 scopus 로고    scopus 로고
    • Maturation of lipoproteins by type II signal peptidase is required for phagosomal escape of Listeria monocytogenes
    • Réglier-Poupet, H., Frehel, C., Dubail, I., Beretti, J.-L., Berche, P., Charbit, A., and Raynaud, C. (2003). Maturation of lipoproteins by type II signal peptidase is required for phagosomal escape of Listeria monocytogenes. J Biol Chem 278, 49469-49477.
    • (2003) J Biol Chem , vol.278 , pp. 49469-49477
    • Réglier-Poupet, H.1    Frehel, C.2    Dubail, I.3    Beretti, J.-L.4    Berche, P.5    Charbit, A.6    Raynaud, C.7
  • 43
    • 77956376824 scopus 로고    scopus 로고
    • Genome-wide analysis and literature-based survey of lipoproteins in Pseudomonas aeruginosa
    • Remans, K., Vercammen, K., Bodilis, J., and Cornelis, P. (2010). Genome-wide analysis and literature-based survey of lipoproteins in Pseudomonas aeruginosa. Microbiology 156, 2597-2607.
    • (2010) Microbiology , vol.156 , pp. 2597-2607
    • Remans, K.1    Vercammen, K.2    Bodilis, J.3    Cornelis, P.4
  • 44
    • 80053612945 scopus 로고    scopus 로고
    • Mutations in Flavobacterium johnsoniae sprE result in defects in gliding motility and protein secretion
    • Rhodes, R. G., Samarasam, M. N., van Groll, E. J., and McBride, M. J. (2011). Mutations in Flavobacterium johnsoniae sprE result in defects in gliding motility and protein secretion. J Bacteriol 193, 5322-5327.
    • (2011) J Bacteriol , vol.193 , pp. 5322-5327
    • Rhodes, R.G.1    Samarasam, M.N.2    van Groll, E.J.3    McBride, M.J.4
  • 45
    • 12544257510 scopus 로고    scopus 로고
    • Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli
    • Robichon, C., Vidal-Ingigliardi, D., and Pugsley, A. P. (2005). Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. J Biol Chem 280, 974-983.
    • (2005) J Biol Chem , vol.280 , pp. 974-983
    • Robichon, C.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 47
    • 0031002075 scopus 로고    scopus 로고
    • Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli
    • Sankaran, K., Gan, K., Rash, B., Qi, H.-Y., Wu, H. C., and Rick, P. D. (1997). Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli. J Bacteriol 179, 2944-2948.
    • (1997) J Bacteriol , vol.179 , pp. 2944-2948
    • Sankaran, K.1    Gan, K.2    Rash, B.3    Qi, H.-Y.4    Wu, H.C.5    Rick, P.D.6
  • 48
    • 0029000609 scopus 로고
    • Modification of bacterial lipoproteins
    • Sankaran, K., Gupta, S. D., and Wu, H. C. (1995). Modification of bacterial lipoproteins. Methods Enzymol 250, 683-697.
    • (1995) Methods Enzymol , vol.250 , pp. 683-697
    • Sankaran, K.1    Gupta, S.D.2    Wu, H.C.3
  • 49
    • 0029027629 scopus 로고
    • Bacterial prolipoprotein signal peptidase
    • Sankaran, K., and Wu, H. C. (1995). Bacterial prolipoprotein signal peptidase. Methods Enzymol 248, 169-180.
    • (1995) Methods Enzymol , vol.248 , pp. 169-180
    • Sankaran, K.1    Wu, H.C.2
  • 50
    • 71749098174 scopus 로고    scopus 로고
    • TLR2 looks at lipoproteins
    • Schenk, M., Belisle, J. T., and Modlin, R. L. (2009). TLR2 looks at lipoproteins. Immunity 31, 847-849.
    • (2009) Immunity , vol.31 , pp. 847-849
    • Schenk, M.1    Belisle, J.T.2    Modlin, R.L.3
  • 51
    • 77952816250 scopus 로고    scopus 로고
    • Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus
    • Schulze, R. J., Chen, S. Y., Kumru, O. S., and Zückert, W. R. (2010). Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus. Mol Microbiol 76, 1266-1278.
    • (2010) Mol Microbiol , vol.76 , pp. 1266-1278
    • Schulze, R.J.1    Chen, S.Y.2    Kumru, O.S.3    Zückert, W.R.4
  • 52
    • 33645077876 scopus 로고    scopus 로고
    • Borrelia burgdorferi lipoproteins are secreted to the outer surface by default
    • Schulze, R. J., and Zückert, W. R. (2006). Borrelia burgdorferi lipoproteins are secreted to the outer surface by default. Mol Microbiol 59, 1473-1484.
    • (2006) Mol Microbiol , vol.59 , pp. 1473-1484
    • Schulze, R.J.1    Zückert, W.R.2
  • 53
    • 55349122529 scopus 로고    scopus 로고
    • Localization and characterization of prolipoprotein diacylglyceryl transferase (Lgt) critical in bacterial lipoprotein biosynthesis
    • Selvan, A. T., and Sankaran, K. (2008). Localization and characterization of prolipoprotein diacylglyceryl transferase (Lgt) critical in bacterial lipoprotein biosynthesis. Biochimie 90, 1647-1655.
    • (2008) Biochimie , vol.90 , pp. 1647-1655
    • Selvan, A.T.1    Sankaran, K.2
  • 55
    • 30744477217 scopus 로고    scopus 로고
    • Lipoprotein computational prediction in spirochaetal genomes
    • Setubal, J. C., Reis, M., Matsunaga, J., and Haake, D. A. (2006). Lipoprotein computational prediction in spirochaetal genomes. Microbiology 152, 113-121.
    • (2006) Microbiology , vol.152 , pp. 113-121
    • Setubal, J.C.1    Reis, M.2    Matsunaga, J.3    Haake, D.A.4
  • 56
    • 77954457475 scopus 로고    scopus 로고
    • TAT-pathway-dependent lipoproteins as a niche-based adaptation in prokaryotes
    • Shruthi, H., Babu, M. M., and Sankaran, K. (2010). TAT-pathway-dependent lipoproteins as a niche-based adaptation in prokaryotes. J Mol Evol 70, 359-370.
    • (2010) J Mol Evol , vol.70 , pp. 359-370
    • Shruthi, H.1    Babu, M.M.2    Sankaran, K.3
  • 57
    • 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 Pohlschröder, M. (2010). Mutational and bioinformatic analysis of haloarchaeal lipobox-containing proteins. Archaea 2010, 410975.
    • (2010) Archaea , vol.2010 , pp. 410975
    • Storf, S.1    Pfeiffer, F.2    Dilks, K.3    Chen, Z.Q.4    Imam, S.5    Pohlschröder, M.6
  • 58
    • 77956988767 scopus 로고    scopus 로고
    • A phylum level perspective on bacterial cell envelope architecture
    • Sutcliffe, I. C. (2010). A phylum level perspective on bacterial cell envelope architecture. Trends Microbiol 18, 464-470.
    • (2010) Trends Microbiol , vol.18 , pp. 464-470
    • Sutcliffe, I.C.1
  • 59
    • 0036066456 scopus 로고    scopus 로고
    • Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes
    • Sutcliffe, I. C., and Harrington, D. J. (2002). Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes. Microbiology 148, 2065-2077.
    • (2002) Microbiology , vol.148 , pp. 2065-2077
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 60
    • 0023177156 scopus 로고
    • Characterization of the sppA gene coding for protease IV, a signal peptide peptidase of Escherichia coli
    • Suzuki, T., Itoh, A., Ichihara, S., and Mizushima, S. (1987). Characterization of the sppA gene coding for protease IV, a signal peptide peptidase of Escherichia coli. J Bacteriol 169, 2523-2528.
    • (1987) J Bacteriol , vol.169 , pp. 2523-2528
    • Suzuki, T.1    Itoh, A.2    Ichihara, S.3    Mizushima, S.4
  • 61
    • 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
  • 62
    • 0033214086 scopus 로고    scopus 로고
    • The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis
    • Tjalsma, H., Zanen, G., Venema, G., Bron, S., and van Dijl, J. M. (1999). The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis. J Biol Chem 274, 28191-28197.
    • (1999) J Biol Chem , vol.274 , pp. 28191-28197
    • Tjalsma, H.1    Zanen, G.2    Venema, G.3    Bron, S.4    van Dijl, J.M.5
  • 63
    • 65349145827 scopus 로고    scopus 로고
    • Biogenesis of outer membranes in Gram-negative bacteria
    • Tokuda, H. (2009). Biogenesis of outer membranes in Gram-negative bacteria. Biosci Biotechnol Biochem 73, 465-473.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 465-473
    • Tokuda, H.1
  • 65
    • 68749109764 scopus 로고    scopus 로고
    • Dissection of LolB function-lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers
    • Tsukahara, J., Mukaiyama, K., Okuda, S., Narita, S.-I., and Tokuda, H. (2009). Dissection of LolB function-lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers. FEBS J 276, 4496-4504.
    • (2009) FEBS J , vol.276 , pp. 4496-4504
    • Tsukahara, J.1    Mukaiyama, K.2    Okuda, S.3    Narita, S.-I.4    Tokuda, H.5
  • 66
    • 33744535529 scopus 로고    scopus 로고
    • Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CyoA
    • van Bloois, E., Haan, G.-J., de Gier, J.-W., Oudega, B., and Luirink, J. (2006). Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CyoA. J Biol Chem 281, 10002-10009.
    • (2006) J Biol Chem , vol.281 , pp. 10002-10009
    • van Bloois, E.1    Haan, G.-J.2    de Gier, J.-W.3    Oudega, B.4    Luirink, J.5
  • 67
    • 34250303119 scopus 로고    scopus 로고
    • Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family
    • Vidal-Ingigliardi, D., Lewenza, S., and Buddelmeijer, N. (2007). Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family. J Bacteriol 189, 4456-4464.
    • (2007) J Bacteriol , vol.189 , pp. 4456-4464
    • Vidal-Ingigliardi, D.1    Lewenza, S.2    Buddelmeijer, N.3


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