메뉴 건너뛰기




Volumn 1828, Issue 11, 2013, Pages 2654-2671

Topological and phylogenetic analyses of bacterial holin families and superfamilies

Author keywords

"Hole forming"; Autolysin; Holin; Phylogeny; Superfamily; Transmembrane pore

Indexed keywords

BACTERIAL PROTEIN; HOLIN; UNCLASSIFIED DRUG;

EID: 84881523856     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.07.004     Document Type: Article
Times cited : (63)

References (52)
  • 1
    • 0029097918 scopus 로고
    • Holins: Form and function in bacteriophage lysis
    • R. Young, and U. Blasi Holins: form and function in bacteriophage lysis FEMS Microbiol. Rev. 17 1995 191 205
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 191-205
    • Young, R.1    Blasi, U.2
  • 2
    • 56149108828 scopus 로고    scopus 로고
    • Protein secretion and membrane insertion systems in bacteria and eukaryotic organelles
    • M.H. Saier, C.H. Ma, L. Rodgers, D.G. Tamang, and M.R. Yen Protein secretion and membrane insertion systems in bacteria and eukaryotic organelles Adv. Appl. Microbiol. 65 2008 141 197
    • (2008) Adv. Appl. Microbiol. , vol.65 , pp. 141-197
    • Saier, M.H.1    Ma, C.H.2    Rodgers, L.3    Tamang, D.G.4    Yen, M.R.5
  • 3
    • 0033768655 scopus 로고    scopus 로고
    • Holins: The protein clocks of bacteriophage infections
    • I.N. Wang, D.L. Smith, and R. Young Holins: the protein clocks of bacteriophage infections Annu. Rev. Microbiol. 54 2000 799 825
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 799-825
    • Wang, I.N.1    Smith, D.L.2    Young, R.3
  • 4
    • 63549137674 scopus 로고    scopus 로고
    • Secretion and subcellular localizations of bacterial proteins: A semantic awareness issue
    • M. Desvaux, M. Hebraud, R. Talon, and I.R. Henderson Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue Trends Microbiol. 17 2009 139 145
    • (2009) Trends Microbiol. , vol.17 , pp. 139-145
    • Desvaux, M.1    Hebraud, M.2    Talon, R.3    Henderson, I.R.4
  • 5
    • 0026800935 scopus 로고
    • Bacteriophage lysis: Mechanism and regulation
    • R. Young Bacteriophage lysis: mechanism and regulation Microbiol. Rev. 56 1992 430 481
    • (1992) Microbiol. Rev. , vol.56 , pp. 430-481
    • Young, R.1
  • 6
    • 84878961038 scopus 로고    scopus 로고
    • Diversity in bacterial lysis systems: Bacteriophages show the way
    • 10.1111/1574-6976.12006
    • M.J. Catalao, F. Gil, J. Moniz-Pereira, C. Sao-Jose, and M. Pimentel Diversity in bacterial lysis systems: bacteriophages show the way FEMS Microbiol. Rev. 37 4 Jul 2012 554 571 10.1111/1574-6976.12006
    • (2012) FEMS Microbiol. Rev. , vol.37 , Issue.4 , pp. 554-571
    • Catalao, M.J.1    Gil, F.2    Moniz-Pereira, J.3    Sao-Jose, C.4    Pimentel, M.5
  • 7
    • 0036132523 scopus 로고    scopus 로고
    • Bacteriophage holins: Deadly diversity
    • R. Young Bacteriophage holins: deadly diversity J. Mol. Microbiol. Biotechnol. 4 2002 21 36
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 21-36
    • Young, R.1
  • 8
    • 51349138721 scopus 로고    scopus 로고
    • Bacteriophage and peptidoglycan degrading enzymes with antimicrobial applications
    • D.M. Donovan Bacteriophage and peptidoglycan degrading enzymes with antimicrobial applications Recent Pat. Biotechnol. 1 2007 113 122
    • (2007) Recent Pat. Biotechnol. , vol.1 , pp. 113-122
    • Donovan, D.M.1
  • 9
    • 77954850130 scopus 로고    scopus 로고
    • The mycobacteriophage Ms6 encodes a chaperone-like protein involved in the endolysin delivery to the peptidoglycan
    • M.J. Catalao, F. Gil, J. Moniz-Pereira, and M. Pimentel The mycobacteriophage Ms6 encodes a chaperone-like protein involved in the endolysin delivery to the peptidoglycan Mol. Microbiol. 77 2010 672 686
    • (2010) Mol. Microbiol. , vol.77 , pp. 672-686
    • Catalao, M.J.1    Gil, F.2    Moniz-Pereira, J.3    Pimentel, M.4
  • 10
    • 33746903479 scopus 로고    scopus 로고
    • The protein secretion systems in Listeria: Inside out bacterial virulence
    • M. Desvaux, and M. Hebraud The protein secretion systems in Listeria: inside out bacterial virulence FEMS Microbiol. Rev. 30 2006 774 805
    • (2006) FEMS Microbiol. Rev. , vol.30 , pp. 774-805
    • Desvaux, M.1    Hebraud, M.2
  • 12
    • 84861673538 scopus 로고    scopus 로고
    • Contribution of holins to protein trafficking: Secretion, leakage or lysis?
    • M. Desvaux Contribution of holins to protein trafficking: secretion, leakage or lysis? Trends Microbiol. 20 2012 259 261
    • (2012) Trends Microbiol. , vol.20 , pp. 259-261
    • Desvaux, M.1
  • 14
    • 0037783318 scopus 로고    scopus 로고
    • Tracing pathways of transport protein evolution
    • M.H. Saier Jr. Tracing pathways of transport protein evolution Mol. Microbiol. 48 2003 1145 1156
    • (2003) Mol. Microbiol. , vol.48 , pp. 1145-1156
    • Saier, Jr.M.H.1
  • 16
    • 33644873454 scopus 로고    scopus 로고
    • TCDB: The Transporter Classification Database for membrane transport protein analyses and information
    • M.H. Saier Jr., C.V. Tran, and R.D. Barabote TCDB: the Transporter Classification Database for membrane transport protein analyses and information Nucleic Acids Res. 34 2006 D181 D186
    • (2006) Nucleic Acids Res. , vol.34
    • Saier, Jr.M.H.1    Tran, C.V.2    Barabote, R.D.3
  • 19
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 25 1997 4876 4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 20
    • 0036132240 scopus 로고    scopus 로고
    • A web-based Tree View (TV) program for the visualization of phylogenetic trees
    • Y. Zhai, J. Tchieu, and M.H. Saier Jr. A web-based Tree View (TV) program for the visualization of phylogenetic trees J. Mol. Microbiol. Biotechnol. 4 2002 69 70
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 69-70
    • Zhai, Y.1    Tchieu, J.2    Saier, Jr.M.H.3
  • 21
    • 84863029391 scopus 로고    scopus 로고
    • Phylogenetic characterization of transport protein superfamilies: Superiority of SuperfamilyTree programs over those based on multiple alignments
    • J.S. Chen, V. Reddy, J.H. Chen, M.A. Shlykov, W.H. Zheng, J. Cho, M.R. Yen, and M.H. Saier Jr. Phylogenetic characterization of transport protein superfamilies: superiority of SuperfamilyTree programs over those based on multiple alignments J. Mol. Microbiol. Biotechnol. 21 2011 83 96
    • (2011) J. Mol. Microbiol. Biotechnol. , vol.21 , pp. 83-96
    • Chen, J.S.1    Reddy, V.2    Chen, J.H.3    Shlykov, M.A.4    Zheng, W.H.5    Cho, J.6    Yen, M.R.7    Saier, Jr.M.H.8
  • 22
    • 70349258246 scopus 로고    scopus 로고
    • Bioinformatic analyses of transmembrane transport: Novel software for deducing protein phylogeny, topology, and evolution
    • M.R. Yen, J. Choi, and M.H. Saier Jr. Bioinformatic analyses of transmembrane transport: novel software for deducing protein phylogeny, topology, and evolution J. Mol. Microbiol. Biotechnol. 17 2009 163 176
    • (2009) J. Mol. Microbiol. Biotechnol. , vol.17 , pp. 163-176
    • Yen, M.R.1    Choi, J.2    Saier, Jr.M.H.3
  • 23
    • 77954892583 scopus 로고    scopus 로고
    • Multidrug resistance: Phylogenetic characterization of superfamilies of secondary carriers that include drug exporters
    • M.R. Yen, J.S. Chen, J.L. Marquez, E.I. Sun, and M.H. Saier Multidrug resistance: phylogenetic characterization of superfamilies of secondary carriers that include drug exporters Methods Mol. Biol. 637 2010 47 64
    • (2010) Methods Mol. Biol. , vol.637 , pp. 47-64
    • Yen, M.R.1    Chen, J.S.2    Marquez, J.L.3    Sun, E.I.4    Saier, M.H.5
  • 24
    • 0034874253 scopus 로고    scopus 로고
    • A web-based program (WHAT) for the simultaneous prediction of hydropathy, amphipathicity, secondary structure and transmembrane topology for a single protein sequence
    • Y. Zhai, and M.H. Saier Jr. A web-based program (WHAT) for the simultaneous prediction of hydropathy, amphipathicity, secondary structure and transmembrane topology for a single protein sequence J. Mol. Microbiol. Biotechnol. 3 2001 501 502
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 501-502
    • Zhai, Y.1    Saier, Jr.M.H.2
  • 25
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • G.E. Tusnady, and I. Simon The HMMTOP transmembrane topology prediction server Bioinformatics 17 2001 849 850
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 26
    • 57249083976 scopus 로고    scopus 로고
    • SPOCTOPUS: A combined predictor of signal peptides and membrane protein topology
    • H. Viklund, A. Bernsel, M. Skwark, and A. Elofsson SPOCTOPUS: a combined predictor of signal peptides and membrane protein topology Bioinformatics 24 2008 2928 2929
    • (2008) Bioinformatics , vol.24 , pp. 2928-2929
    • Viklund, H.1    Bernsel, A.2    Skwark, M.3    Elofsson, A.4
  • 27
    • 0035087954 scopus 로고    scopus 로고
    • A web-based program for the prediction of average hydropathy, average amphipathicity and average similarity of multiply aligned homologous proteins
    • Y. Zhai, and M.H. Saier Jr. A web-based program for the prediction of average hydropathy, average amphipathicity and average similarity of multiply aligned homologous proteins J. Mol. Microbiol. Biotechnol. 3 2001 285 286
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 285-286
    • Zhai, Y.1    Saier, Jr.M.H.2
  • 29
    • 0029962489 scopus 로고    scopus 로고
    • ParaMEME: A parallel implementation and a web interface for a DNA and protein motif discovery tool
    • W.N. Grundy, T.L. Bailey, and C.P. Elkan ParaMEME: a parallel implementation and a web interface for a DNA and protein motif discovery tool Comput. Appl. Biosci. 12 1996 303 310
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 303-310
    • Grundy, W.N.1    Bailey, T.L.2    Elkan, C.P.3
  • 31
    • 0035988281 scopus 로고    scopus 로고
    • A simple sensitive program for detecting internal repeats in sets of multiply aligned homologous proteins
    • Y. Zhai, and M.H. Saier Jr. A simple sensitive program for detecting internal repeats in sets of multiply aligned homologous proteins J. Mol. Microbiol. Biotechnol. 4 2002 375 377
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 375-377
    • Zhai, Y.1    Saier, Jr.M.H.2
  • 32
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • J. Devereux, P. Haeberli, and O. Smithies A comprehensive set of sequence analysis programs for the VAX Nucleic Acids Res. 12 1984 387 395
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 33
    • 84861185139 scopus 로고    scopus 로고
    • BioV Suite - A collection of programs for the study of transport protein evolution
    • V.S. Reddy, and M.H. Saier Jr. BioV Suite - a collection of programs for the study of transport protein evolution FEBS J. 279 2012 2036 2046
    • (2012) FEBS J. , vol.279 , pp. 2036-2046
    • Reddy, V.S.1    Saier, Jr.M.H.2
  • 34
    • 0023656052 scopus 로고
    • Dynamics of proteoliposome formation. Intermediate states during detergent dialysis
    • J.M. Wrigglesworth, M.S. Wooster, J. Elsden, and H.J. Danneel Dynamics of proteoliposome formation. Intermediate states during detergent dialysis Biochem. J. 246 1987 737 744
    • (1987) Biochem. J. , vol.246 , pp. 737-744
    • Wrigglesworth, J.M.1    Wooster, M.S.2    Elsden, J.3    Danneel, H.J.4
  • 35
  • 36
    • 0028345374 scopus 로고
    • Computer-aided analyses of transport protein sequences: Gleaning evidence concerning function, structure, biogenesis, and evolution
    • M.H. Saier Jr. Computer-aided analyses of transport protein sequences: gleaning evidence concerning function, structure, biogenesis, and evolution Microbiol. Rev. 58 1994 71 93
    • (1994) Microbiol. Rev. , vol.58 , pp. 71-93
    • Saier, Jr.M.H.1
  • 37
    • 0041737777 scopus 로고    scopus 로고
    • Reversing transmembrane electron flow: The DsbD and DsbB protein families
    • R.A. Kimball, L. Martin, and M.H. Saier Jr. Reversing transmembrane electron flow: the DsbD and DsbB protein families J. Mol. Microbiol. Biotechnol. 5 2003 133 149
    • (2003) J. Mol. Microbiol. Biotechnol. , vol.5 , pp. 133-149
    • Kimball, R.A.1    Martin, L.2    Saier, Jr.M.H.3
  • 38
    • 0027160122 scopus 로고
    • The mitochondrial carrier family of transport proteins: Structural, functional, and evolutionary relationships
    • J. Kuan, and M.H. Saier Jr. The mitochondrial carrier family of transport proteins: structural, functional, and evolutionary relationships Crit. Rev. Biochem. Mol. Biol. 28 1993 209 233
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 209-233
    • Kuan, J.1    Saier, Jr.M.H.2
  • 39
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the MIP family of transmembrane channel proteins
    • J.H. Park, and M.H. Saier Jr. Phylogenetic characterization of the MIP family of transmembrane channel proteins J. Membr. Biol. 153 1996 171 180
    • (1996) J. Membr. Biol. , vol.153 , pp. 171-180
    • Park, J.H.1    Saier, Jr.M.H.2
  • 41
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • G. von Heijne Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule J. Mol. Biol. 225 1992 487 494
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 42
    • 0028364507 scopus 로고
    • Membrane protein topology: Effects of delta mu H + on the translocation of charged residues explain the 'positive inside' rule
    • H. Andersson, and G. von Heijne Membrane protein topology: effects of delta mu H + on the translocation of charged residues explain the 'positive inside' rule EMBO J. 13 1994 2267 2272
    • (1994) EMBO J. , vol.13 , pp. 2267-2272
    • Andersson, H.1    Von Heijne, G.2
  • 43
    • 24644490119 scopus 로고    scopus 로고
    • Comparative analysis of amino acid distributions in integral membrane proteins from 107 genomes
    • J. Nilsson, B. Persson, and G. von Heijne Comparative analysis of amino acid distributions in integral membrane proteins from 107 genomes Proteins 60 2005 606 616
    • (2005) Proteins , vol.60 , pp. 606-616
    • Nilsson, J.1    Persson, B.2    Von Heijne, G.3
  • 45
    • 0342980358 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for three transmembrane domains in the class i holin, lambda S
    • A. Grundling, U. Blasi, and R. Young Biochemical and genetic evidence for three transmembrane domains in the class I holin, lambda S J. Biol. Chem. 275 2000 769 776
    • (2000) J. Biol. Chem. , vol.275 , pp. 769-776
    • Grundling, A.1    Blasi, U.2    Young, R.3
  • 46
    • 0032835864 scopus 로고    scopus 로고
    • The ability of "low G + C gram-positive" ruminal bacteria to resist monensin and counteract potassium depletion
    • T.R. Callaway, K.A. Adams, and J.B. Russell The ability of "low G + C gram-positive" ruminal bacteria to resist monensin and counteract potassium depletion Curr. Microbiol. 39 1999 226 230
    • (1999) Curr. Microbiol. , vol.39 , pp. 226-230
    • Callaway, T.R.1    Adams, K.A.2    Russell, J.B.3
  • 48
    • 0035819875 scopus 로고    scopus 로고
    • Genetic analysis of the T4 holin: Timing and topology
    • E. Ramanculov, and R. Young Genetic analysis of the T4 holin: timing and topology Gene 265 2001 25 36
    • (2001) Gene , vol.265 , pp. 25-36
    • Ramanculov, E.1    Young, R.2
  • 49
    • 25144505528 scopus 로고    scopus 로고
    • Periplasmic domains define holin-antiholin interactions in t4 lysis inhibition
    • T.A. Tran, D.K. Struck, and R. Young Periplasmic domains define holin-antiholin interactions in t4 lysis inhibition J. Bacteriol. 187 2005 6631 6640
    • (2005) J. Bacteriol. , vol.187 , pp. 6631-6640
    • Tran, T.A.1    Struck, D.K.2    Young, R.3
  • 50
    • 75149113312 scopus 로고    scopus 로고
    • The N-terminal transmembrane domain of lambda S is required for holin but not antiholin function
    • R. White, T.A. Tran, C.A. Dankenbring, J. Deaton, and R. Young The N-terminal transmembrane domain of lambda S is required for holin but not antiholin function J. Bacteriol. 192 2010 725 733
    • (2010) J. Bacteriol. , vol.192 , pp. 725-733
    • White, R.1    Tran, T.A.2    Dankenbring, C.A.3    Deaton, J.4    Young, R.5
  • 51


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.