메뉴 건너뛰기




Volumn 588, Issue 23, 2014, Pages 4325-4333

Clostridium difficile sortase recognizes a (S/P)PXTG sequence motif and can accommodate diaminopimelic acid as a substrate for transpeptidation

Author keywords

Adhesion; Diaminopimelic acid; Mass spectrometry; Peptidoglycan; Transpeptidation; Virulence

Indexed keywords

DIAMINOPIMELIC ACID; SORTASE; AMINOACYLTRANSFERASE; BACTERIAL PROTEIN; CYSTEINE PROTEINASE; PEPTIDE; PROTEIN BINDING; RECOMBINANT PROTEIN; SORTASE A;

EID: 84910664729     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.09.041     Document Type: Article
Times cited : (19)

References (43)
  • 1
    • 33645049557 scopus 로고    scopus 로고
    • Protein cell surface display in Gram-positive bacteria: From single protein to macromolecular protein structure
    • M. Desvaux, E. Dumas, I. Chafsey, and M. Hebraud Protein cell surface display in Gram-positive bacteria: from single protein to macromolecular protein structure FEMS Microbiol. Lett. 256 2006 1 15
    • (2006) FEMS Microbiol. Lett. , vol.256 , pp. 1-15
    • Desvaux, M.1    Dumas, E.2    Chafsey, I.3    Hebraud, M.4
  • 3
    • 79951816315 scopus 로고    scopus 로고
    • Architects at the bacterial surface - Sortases and the assembly of pili with isopeptide bonds
    • A.P. Hendrickx, J.M. Budzik, S.Y. Oh, and O. Schneewind Architects at the bacterial surface - sortases and the assembly of pili with isopeptide bonds Nat. Rev. Microbiol. 9 2011 166 176
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 166-176
    • Hendrickx, A.P.1    Budzik, J.M.2    Oh, S.Y.3    Schneewind, O.4
  • 4
    • 33645137247 scopus 로고    scopus 로고
    • Sortases and the art of anchoring proteins to the envelopes of Gram-positive bacteria
    • L.A. Marraffini, A.C. DeDent, and O. Schneewind Sortases and the art of anchoring proteins to the envelopes of Gram-positive bacteria Microbiol. Mol. Biol. Rev. 70 2006 192 221
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 192-221
    • Marraffini, L.A.1    Dedent, A.C.2    Schneewind, O.3
  • 5
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of Gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • W.W. Navarre, and O. Schneewind Surface proteins of Gram-positive bacteria and mechanisms of their targeting to the cell wall envelope Microbiol. Mol. Biol. Rev. 63 1999 174 229
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 6
    • 29144477176 scopus 로고    scopus 로고
    • Bacterial cell wall synthesis: New insights from localization studies
    • D.J. Scheffers, and M.G. Pinho Bacterial cell wall synthesis: new insights from localization studies Microbiol. Mol. Biol. Rev. 69 2005 585 607
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 585-607
    • Scheffers, D.J.1    Pinho, M.G.2
  • 7
    • 8844240627 scopus 로고    scopus 로고
    • Protein sorting to the cell wall envelope of Gram-positive bacteria
    • H. Ton-That, L.A. Marraffini, and O. Schneewind Protein sorting to the cell wall envelope of Gram-positive bacteria Biochim. Biophys. Acta 1694 2004 269 278
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 269-278
    • Ton-That, H.1    Marraffini, L.A.2    Schneewind, O.3
  • 8
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • S.K. Mazmanian, G. Liu, H. Ton-That, and O. Schneewind Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall Science 285 1999 760 763
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 9
    • 0033607265 scopus 로고    scopus 로고
    • Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif
    • H. Ton-That, G. Liu, S.K. Mazmanian, K.F. Faull, and O. Schneewind Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif Proc. Natl. Acad. Sci. USA 96 1999 12424 12429
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12424-12429
    • Ton-That, H.1    Liu, G.2    Mazmanian, S.K.3    Faull, K.F.4    Schneewind, O.5
  • 10
    • 2142808787 scopus 로고    scopus 로고
    • A comparative genome analysis identifies distinct sorting pathways in Gram-positive bacteria
    • D. Comfort, and R.T. Clubb A comparative genome analysis identifies distinct sorting pathways in Gram-positive bacteria Infect. Immun. 72 2004 2710 2722
    • (2004) Infect. Immun. , vol.72 , pp. 2710-2722
    • Comfort, D.1    Clubb, R.T.2
  • 11
  • 12
    • 82155168216 scopus 로고    scopus 로고
    • Sortase enzymes in Gram-positive bacteria
    • T. Spirig, E.M. Weiner, and R.T. Clubb Sortase enzymes in Gram-positive bacteria Mol. Microbiol. 82 2011 1044 1059
    • (2011) Mol. Microbiol. , vol.82 , pp. 1044-1059
    • Spirig, T.1    Weiner, E.M.2    Clubb, R.T.3
  • 15
    • 0032582528 scopus 로고    scopus 로고
    • Anchor structure of staphylococcal surface proteins. III. Role of the FemA, FemB, and FemX factors in anchoring surface proteins to the bacterial cell wall
    • H. Ton-That, H. Labischinski, B. Berger-Bachi, and O. Schneewind Anchor structure of staphylococcal surface proteins. III. Role of the FemA, FemB, and FemX factors in anchoring surface proteins to the bacterial cell wall J. Biol. Chem. 273 1998 29143 29149
    • (1998) J. Biol. Chem. , vol.273 , pp. 29143-29149
    • Ton-That, H.1    Labischinski, H.2    Berger-Bachi, B.3    Schneewind, O.4
  • 16
    • 0037589849 scopus 로고    scopus 로고
    • Kinetic and mechanistic characterization of recombinant Lactobacillus viridescens FemX (UDP-N-acetylmuramoyl pentapeptide-lysine N6-alanyltransferase)
    • S.S. Hegde, and J.S. Blanchard Kinetic and mechanistic characterization of recombinant Lactobacillus viridescens FemX (UDP-N-acetylmuramoyl pentapeptide-lysine N6-alanyltransferase) J. Biol. Chem. 278 2003 22861 22867
    • (2003) J. Biol. Chem. , vol.278 , pp. 22861-22867
    • Hegde, S.S.1    Blanchard, J.S.2
  • 18
    • 0033588339 scopus 로고    scopus 로고
    • Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction
    • H. Ton-That, and O. Schneewind Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction J. Biol. Chem. 274 1999 24316 24320
    • (1999) J. Biol. Chem. , vol.274 , pp. 24316-24320
    • Ton-That, H.1    Schneewind, O.2
  • 20
    • 61349088032 scopus 로고    scopus 로고
    • Cell wall anchor structure of BcpA pili in Bacillus anthracis
    • J.M. Budzik, S.Y. Oh, and O. Schneewind Cell wall anchor structure of BcpA pili in Bacillus anthracis J. Biol. Chem. 283 2008 36676 36686
    • (2008) J. Biol. Chem. , vol.283 , pp. 36676-36686
    • Budzik, J.M.1    Oh, S.Y.2    Schneewind, O.3
  • 21
    • 0034603801 scopus 로고    scopus 로고
    • Anchor structure of cell wall surface proteins in Listeria monocytogenes
    • G. Dhar, K.F. Faull, and O. Schneewind Anchor structure of cell wall surface proteins in Listeria monocytogenes Biochemistry 39 2000 3725 3733
    • (2000) Biochemistry , vol.39 , pp. 3725-3733
    • Dhar, G.1    Faull, K.F.2    Schneewind, O.3
  • 22
    • 21844433171 scopus 로고    scopus 로고
    • Genome-wide detection and analysis of cell wall-bound proteins with LPxTG-like sorting motifs
    • J. Boekhorst, M.W. de Been, M. Kleerebezem, and R.J. Siezen Genome-wide detection and analysis of cell wall-bound proteins with LPxTG-like sorting motifs J. Bacteriol. 187 2005 4928 4934
    • (2005) J. Bacteriol. , vol.187 , pp. 4928-4934
    • Boekhorst, J.1    De Been, M.W.2    Kleerebezem, M.3    Siezen, R.J.4
  • 23
    • 67649391053 scopus 로고    scopus 로고
    • Clostridium difficile infection: New developments in epidemiology and pathogenesis
    • M. Rupnik, M.H. Wilcox, and D.N. Gerding Clostridium difficile infection: new developments in epidemiology and pathogenesis Nat. Rev. Microbiol. 7 2009 526 536
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 526-536
    • Rupnik, M.1    Wilcox, M.H.2    Gerding, D.N.3
  • 29
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • L.A. Kelley, and M.J. Sternberg Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 31
    • 69949151708 scopus 로고    scopus 로고
    • The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized
    • N. Suree, C.K. Liew, V.A. Villareal, W. Thieu, E.A. Fadeev, J.J. Clemens, M.E. Jung, and R.T. Clubb The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized J. Biol. Chem. 284 2009 24465 24477
    • (2009) J. Biol. Chem. , vol.284 , pp. 24465-24477
    • Suree, N.1    Liew, C.K.2    Villareal, V.A.3    Thieu, W.4    Fadeev, E.A.5    Clemens, J.J.6    Jung, M.E.7    Clubb, R.T.8
  • 32
    • 0027442464 scopus 로고
    • Cell wall sorting signals in surface proteins of Gram-positive bacteria
    • O. Schneewind, D. Mihaylova-Petkov, and P. Model Cell wall sorting signals in surface proteins of Gram-positive bacteria EMBO J. 12 1993 4803 4811
    • (1993) EMBO J. , vol.12 , pp. 4803-4811
    • Schneewind, O.1    Mihaylova-Petkov, D.2    Model, P.3
  • 33
    • 0035932982 scopus 로고    scopus 로고
    • Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus
    • U. Ilangovan, H. Ton-That, J. Iwahara, O. Schneewind, and R.T. Clubb Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus Proc. Natl. Acad. Sci. USA 98 2001 6056 6061
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6056-6061
    • Ilangovan, U.1    Ton-That, H.2    Iwahara, J.3    Schneewind, O.4    Clubb, R.T.5
  • 34
    • 80051695335 scopus 로고    scopus 로고
    • Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links
    • J. Peltier, P. Courtin, I. El Meouche, L. Lemee, M.P. Chapot-Chartier, and J.L. Pons Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links J. Biol. Chem. 286 2011 29053 29062
    • (2011) J. Biol. Chem. , vol.286 , pp. 29053-29062
    • Peltier, J.1    Courtin, P.2    El Meouche, I.3    Lemee, L.4    Chapot-Chartier, M.P.5    Pons, J.L.6
  • 35
    • 0034737451 scopus 로고    scopus 로고
    • Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Sortase catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH(2)-Gly(3) substrates
    • H. Ton-That, S.K. Mazmanian, K.F. Faull, and O. Schneewind Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Sortase catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH(2)-Gly(3) substrates J. Biol. Chem. 275 2000 9876 9881
    • (2000) J. Biol. Chem. , vol.275 , pp. 9876-9881
    • Ton-That, H.1    Mazmanian, S.K.2    Faull, K.F.3    Schneewind, O.4
  • 36
    • 23944522769 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase transpeptidase SrtA: Insight into the kinetic mechanism and evidence for a reverse protonation catalytic mechanism
    • B.A. Frankel, R.G. Kruger, D.E. Robinson, N.L. Kelleher, and D.G. McCafferty Staphylococcus aureus sortase transpeptidase SrtA: insight into the kinetic mechanism and evidence for a reverse protonation catalytic mechanism Biochemistry 44 2005 11188 11200
    • (2005) Biochemistry , vol.44 , pp. 11188-11200
    • Frankel, B.A.1    Kruger, R.G.2    Robinson, D.E.3    Kelleher, N.L.4    McCafferty, D.G.5
  • 39
    • 33644984956 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase A transpeptidase. Calcium promotes sorting signal binding by altering the mobility and structure of an active site loop
    • M.T. Naik, N. Suree, U. Ilangovan, C.K. Liew, W. Thieu, D.O. Campbell, J.J. Clemens, M.E. Jung, and R.T. Clubb Staphylococcus aureus sortase A transpeptidase. Calcium promotes sorting signal binding by altering the mobility and structure of an active site loop J. Biol. Chem. 281 2006 1817 1826
    • (2006) J. Biol. Chem. , vol.281 , pp. 1817-1826
    • Naik, M.T.1    Suree, N.2    Ilangovan, U.3    Liew, C.K.4    Thieu, W.5    Campbell, D.O.6    Clemens, J.J.7    Jung, M.E.8    Clubb, R.T.9
  • 41
    • 43049135194 scopus 로고    scopus 로고
    • Agr-mediated dispersal of Staphylococcus aureus biofilms
    • B.R. Boles, and A.R. Horswill Agr-mediated dispersal of Staphylococcus aureus biofilms PLoS Pathog. 4 2008 e1000052
    • (2008) PLoS Pathog. , vol.4 , pp. 1000052
    • Boles, B.R.1    Horswill, A.R.2
  • 42
    • 0035839473 scopus 로고    scopus 로고
    • Loss of clumping factor B fibrinogen binding activity by Staphylococcus aureus involves cessation of transcription, shedding and cleavage by metalloprotease
    • F.M. McAleese, E.J. Walsh, M. Sieprawska, J. Potempa, and T.J. Foster Loss of clumping factor B fibrinogen binding activity by Staphylococcus aureus involves cessation of transcription, shedding and cleavage by metalloprotease J. Biol. Chem. 276 2001 29969 29978
    • (2001) J. Biol. Chem. , vol.276 , pp. 29969-29978
    • McAleese, F.M.1    Walsh, E.J.2    Sieprawska, M.3    Potempa, J.4    Foster, T.J.5
  • 43
    • 80052328723 scopus 로고    scopus 로고
    • The Fsr quorum-sensing system of Enterococcus faecalis modulates surface display of the collagen-binding MSCRAMM Ace through regulation of gelE
    • K.L. Pinkston, P. Gao, D. Diaz-Garcia, J. Sillanpaa, S.R. Nallapareddy, B.E. Murray, and B.R. Harvey The Fsr quorum-sensing system of Enterococcus faecalis modulates surface display of the collagen-binding MSCRAMM Ace through regulation of gelE J. Bacteriol. 193 2011 4317 4325
    • (2011) J. Bacteriol. , vol.193 , pp. 4317-4325
    • Pinkston, K.L.1    Gao, P.2    Diaz-Garcia, D.3    Sillanpaa, J.4    Nallapareddy, S.R.5    Murray, B.E.6    Harvey, B.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.