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Volumn 7, Issue 2, 2017, Pages 741-753

Genetic analysis of the lambda spanins Rz and Rz1: Identification of functional domains

Author keywords

Escherichia coli; Lysis; Membrane fusion; Phage

Indexed keywords

ALLELE; BACTERIOPHAGE; COMPLEX FORMATION; COMPRESSION; DNA STRUCTURE; ESCHERICHIA COLI; GENETIC ANALYSIS; GENETICS; HUMAN; IN VITRO STUDY; LYSIS; MEMBRANE FUSION; MISSENSE MUTATION; MUTAGENESIS; NONHUMAN; PROTEIN DOMAIN; READING FRAME; AMINO ACID SEQUENCE; ENTEROBACTERIA PHAGE LAMBDA; MUTATION; VIROLOGY;

EID: 85012864552     PISSN: None     EISSN: 21601836     Source Type: Journal    
DOI: 10.1534/g3.116.037192     Document Type: Article
Times cited : (15)

References (39)
  • 1
    • 0035967522 scopus 로고    scopus 로고
    • Buried polar residues in coiled-coil interfaces
    • Akey, D. L., V. N. Malashkevich, and P. S. Kim, 2001 Buried polar residues in coiled-coil interfaces. Biochemistry 40(21): 6352-6360.
    • (2001) Biochemistry , vol.40 , Issue.21 , pp. 6352-6360
    • Akey, D.L.1    Malashkevich, V.N.2    Kim, P.S.3
  • 3
    • 52649112247 scopus 로고    scopus 로고
    • The final step in the phage infection cycle: the Rz and Rz1 lysis proteins link the inner and outer membranes
    • Berry, J., E. J. Summer, D. K. Struck, and R. Young, 2008 The final step in the phage infection cycle: the Rz and Rz1 lysis proteins link the inner and outer membranes. Mol. Microbiol. 70(2): 341-351.
    • (2008) Mol. Microbiol , vol.70 , Issue.2 , pp. 341-351
    • Berry, J.1    Summer, E.J.2    Struck, D.K.3    Young, R.4
  • 4
    • 77957307926 scopus 로고    scopus 로고
    • The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation
    • Berry, J., C. Savva, A. Holzenburg, and R. Young, 2010 The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation. Protein Sci. 19(10): 1967-1977.
    • (2010) Protein Sci , vol.19 , Issue.10 , pp. 1967-1977
    • Berry, J.1    Savva, C.2    Holzenburg, A.3    Young, R.4
  • 6
    • 84868557725 scopus 로고    scopus 로고
    • The spanin complex is essential for lambda lysis
    • Berry, J. D., M. Rajaure, T. Pang, and R. Young, 2012 The spanin complex is essential for lambda lysis. J. Bacteriol. 194: 5667-5674.
    • (2012) J. Bacteriol , vol.194 , pp. 5667-5674
    • Berry, J.D.1    Rajaure, M.2    Pang, T.3    Young, R.4
  • 7
    • 84875584251 scopus 로고    scopus 로고
    • Spanin function requires subunit homodimerization through intermolecular disulfide bonds
    • Berry, J. D., M. Rajaure, and R. Young, 2013 Spanin function requires subunit homodimerization through intermolecular disulfide bonds. Mol. Microbiol. 88(1): 35-47.
    • (2013) Mol. Microbiol , vol.88 , Issue.1 , pp. 35-47
    • Berry, J.D.1    Rajaure, M.2    Young, R.3
  • 9
    • 0000882208 scopus 로고
    • Hypothesis about the function of membrane-buried proline residues in transport proteins
    • Brandl, C. J., and C. M. Deber, 1986 Hypothesis about the function of membrane-buried proline residues in transport proteins. Proc. Natl. Acad. Sci. USA 83(4): 917-921.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , Issue.4 , pp. 917-921
    • Brandl, C.J.1    Deber, C.M.2
  • 10
    • 0345276226 scopus 로고    scopus 로고
    • Biopython: Python tools for computational biology
    • Chapman, B., and J. Chang, 2000 Biopython: Python tools for computational biology. ACM Sigbio Newsletter 20(2): 15-19.
    • (2000) ACM Sigbio Newsletter , vol.20 , Issue.2 , pp. 15-19
    • Chapman, B.1    Chang, J.2
  • 12
    • 80052746513 scopus 로고    scopus 로고
    • Proline in transmembrane domain of type II protein DPP-IV governs its translocation behavior through endoplasmic reticulum
    • Chung, K.-M., C.-H. Huang, J.-H. Cheng, C.-H. Tsai, C.-S. Suen et al., 2011 Proline in transmembrane domain of type II protein DPP-IV governs its translocation behavior through endoplasmic reticulum. Biochemistry 50(37): 7909-7918.
    • (2011) Biochemistry , vol.50 , Issue.37 , pp. 7909-7918
    • Chung, K.-M.1    Huang, C.-H.2    Cheng, J.-H.3    Tsai, C.-H.4    Suen, C.-S.5
  • 13
    • 84979854249 scopus 로고    scopus 로고
    • JPred4: a protein secondary structure prediction server
    • Drozdetskiy, A., C. Cole, J. Procter, and G. J. Barton, 2015 JPred4: a protein secondary structure prediction server. Nucleic Acids Res. 43: W389-W394.
    • (2015) Nucleic Acids Res , vol.43 , pp. W389-W394
    • Drozdetskiy, A.1    Cole, C.2    Procter, J.3    Barton, G.J.4
  • 14
    • 0033758762 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of dimer and oligomer interactions of the λ S holin
    • Gründling, A., U. Bläsi, and R. Young, 2000 Genetic and biochemical analysis of dimer and oligomer interactions of the λ S holin. J. Bacteriol. 182(21): 6082-6090.
    • (2000) J. Bacteriol , vol.182 , Issue.21 , pp. 6082-6090
    • Gründling, A.1    Bläsi, U.2    Young, R.3
  • 16
    • 84877130070 scopus 로고    scopus 로고
    • Construction and analysis of randomized protein-encoding libraries using error-prone PCR
    • Ed. 2. Humana Press, New York, NY
    • Hanson-Manful, P., and W. M. Patrick, 2013 Construction and analysis of randomized protein-encoding libraries using error-prone PCR, pp. 251-267 in Protein Nanotechnology: Protocols, Instrumentation, and Applications, Ed. 2. Humana Press, New York, NY.
    • (2013) Protein Nanotechnology: Protocols, Instrumentation, and Applications , pp. 251-267
    • Hanson-Manful, P.1    Patrick, W.M.2
  • 17
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison, S. C., 2008 Viral membrane fusion. Nat. Struct. Mol. Biol. 15(7): 690-698.
    • (2008) Nat. Struct. Mol. Biol , vol.15 , Issue.7 , pp. 690-698
    • Harrison, S.C.1
  • 19
    • 0342655941 scopus 로고    scopus 로고
    • The Rz1 gene product of bacteriophage lambda is a lipoprotein localized in the outer membrane of Escherichia coli
    • Kedzierska, S., A. Wawrzynow, and A. Taylor, 1996 The Rz1 gene product of bacteriophage lambda is a lipoprotein localized in the outer membrane of Escherichia coli. Gene 168: 1-8.
    • (1996) Gene , vol.168 , pp. 1-8
    • Kedzierska, S.1    Wawrzynow, A.2    Taylor, A.3
  • 20
    • 85017019017 scopus 로고    scopus 로고
    • Mechanisms of virus membrane fusion proteins
    • Kielian, M., 2014 Mechanisms of virus membrane fusion proteins. Annu. Rev. Virol. 1(1): 171-189.
    • (2014) Annu. Rev. Virol , vol.1 , Issue.1 , pp. 171-189
    • Kielian, M.1
  • 21
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., M. Van Dyke, and J. Stock, 1991 Predicting coiled coils from protein sequences. Science 252(5009): 1162-1164.
    • (1991) Science , vol.252 , Issue.5009 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 23
    • 77954692040 scopus 로고    scopus 로고
    • Sorting of bacterial lipoproteins to the outer membrane by the Lol system
    • Narita, S., and H. Tokuda, 2010 Sorting of bacterial lipoproteins to the outer membrane by the Lol system. Methods Mol. Biol. 619: 117-129.
    • (2010) Methods Mol. Biol , vol.619 , pp. 117-129
    • Narita, S.1    Tokuda, H.2
  • 24
    • 77950211683 scopus 로고    scopus 로고
    • Mutational analysis of the S21 pinholin
    • Pang, T., T. Park, and R. Young, 2010 Mutational analysis of the S21 pinholin. Mol. Microbiol. 76: 68-77.
    • (2010) Mol. Microbiol , vol.76 , pp. 68-77
    • Pang, T.1    Park, T.2    Young, R.3
  • 25
    • 33845940948 scopus 로고    scopus 로고
    • Topological dynamics of holins in programmed bacterial lysis
    • Park, T., D. K. Struck, J. F. Deaton, and R. Young, 2006 Topological dynamics of holins in programmed bacterial lysis. Proc. Natl. Acad. Sci. USA 103(52): 19713-19718.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.52 , pp. 19713-19718
    • Park, T.1    Struck, D.K.2    Deaton, J.F.3    Young, R.4
  • 26
    • 0020446736 scopus 로고
    • Coiled-coils in α-helix-containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins
    • Parry, D. A., 1982 Coiled-coils in α-helix-containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins. Biosci. Rep. 2(12): 1017-1024.
    • (1982) Biosci. Rep , vol.2 , Issue.12 , pp. 1017-1024
    • Parry, D.A.1
  • 27
    • 84922359615 scopus 로고    scopus 로고
    • Virus and cell fusion mechanisms
    • Podbilewicz, B., 2014 Virus and cell fusion mechanisms. Annu. Rev. Cell Dev. Biol. 30(1): 111-139.
    • (2014) Annu. Rev. Cell Dev. Biol , vol.30 , Issue.1 , pp. 111-139
    • Podbilewicz, B.1
  • 29
    • 0035819875 scopus 로고    scopus 로고
    • Genetic analysis of the T4 holin: timing and topology
    • Ramanculov, E. R., and R. Young, 2001 Genetic analysis of the T4 holin: timing and topology. Gene 265: 25-36.
    • (2001) Gene , vol.265 , pp. 25-36
    • Ramanculov, E.R.1    Young, R.2
  • 30
    • 84874033858 scopus 로고    scopus 로고
    • Linkers in the structural biology of protein-protein interactions
    • Reddy Chichili, V. P., V. Kumar, and J. Sivaraman, 2013 Linkers in the structural biology of protein-protein interactions. Protein Sci. 22(2): 153-167.
    • (2013) Protein Sci , vol.22 , Issue.2 , pp. 153-167
    • Reddy Chichili, V.P.1    Kumar, V.2    Sivaraman, J.3
  • 31
    • 84891152665 scopus 로고    scopus 로고
    • Stable micron-scale holes are a general feature of canonical holins
    • Savva, C. G., J. S. Dewey, S. H. Moussa, K. H. To, A. Holzenburg et al., 2014 Stable micron-scale holes are a general feature of canonical holins. Mol. Microbiol. 91(1): 57-65.
    • (2014) Mol. Microbiol , vol.91 , Issue.1 , pp. 57-65
    • Savva, C.G.1    Dewey, J.S.2    Moussa, S.H.3    To, K.H.4    Holzenburg, A.5
  • 32
    • 33846577339 scopus 로고    scopus 로고
    • Kinking the coiled coil-negatively charged residues at the coiled-coil interface
    • Straussman, R., A. Ben-Ya'acov, D. N.Woolfson, and S. Ravid, 2007 Kinking the coiled coil-negatively charged residues at the coiled-coil interface. J. Mol. Biol. 366(4): 1232-1242.
    • (2007) J. Mol. Biol , vol.366 , Issue.4 , pp. 1232-1242
    • Straussman, R.1    Ben-Ya'acov, A.2    Woolfson, D.N.3    Ravid, S.4
  • 33
    • 35048873167 scopus 로고    scopus 로고
    • Rz/Rz1 lysis gene equivalents in phages of gram-negative hosts
    • Summer, E. J., J. Berry, T. A. Tran, L. Niu, D. K. Struck et al., 2007 Rz/Rz1 lysis gene equivalents in phages of gram-negative hosts. J. Mol. Biol. 373 (5): 1098-1112.
    • (2007) J. Mol. Biol , vol.373 , Issue.5 , pp. 1098-1112
    • Summer, E.J.1    Berry, J.2    Tran, T.A.3    Niu, L.4    Struck, D.K.5
  • 34
    • 84856289583 scopus 로고    scopus 로고
    • Cell-cell membrane fusion induced by p15 fusion-associated small transmembrane (FAST) protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix
    • Top, D., J. A. Read, S. J. Dawe, R. T. Syvitski, and R. Duncan, 2012 Cell-cell membrane fusion induced by p15 fusion-associated small transmembrane (FAST) protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix. J. Biol. Chem. 287(5): 3403-3414.
    • (2012) J. Biol. Chem , vol.287 , Issue.5 , pp. 3403-3414
    • Top, D.1    Read, J.A.2    Dawe, S.J.3    Syvitski, R.T.4    Duncan, R.5
  • 35
    • 0035795721 scopus 로고    scopus 로고
    • Amino acid distributions in integral membrane protein structures
    • Ulmschneider, M. B., and M. S. Sansom, 2001 Amino acid distributions in integral membrane protein structures. Biochim. Biophys. Acta 1512(1): 1-14.
    • (2001) Biochim. Biophys. Acta , vol.1512 , Issue.1 , pp. 1-14
    • Ulmschneider, M.B.1    Sansom, M.S.2
  • 36
    • 0021856417 scopus 로고
    • Signal sequences: the limits of variation
    • Von Heijne, G., 1985 Signal sequences: the limits of variation. J. Mol. Biol. 184(1): 99-105.
    • (1985) J. Mol. Biol , vol.184 , Issue.1 , pp. 99-105
    • Von Heijne, G.1
  • 37
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: minimal machinery for membrane fusion
    • Weber, T., B. V. Zemelman, J. A. McNew, B. Westermann, M. Gmachl et al., 1998 SNAREpins: minimal machinery for membrane fusion. Cell 92(6): 759-772.
    • (1998) Cell , vol.92 , Issue.6 , pp. 759-772
    • Weber, T.1    Zemelman, B.V.2    McNew, J.A.3    Westermann, B.4    Gmachl, M.5
  • 38
    • 0026800935 scopus 로고
    • Bacteriophage lysis: mechanism and regulation
    • Young, R., 1992 Bacteriophage lysis: mechanism and regulation. Microbiol. Rev. 56: 430-481.
    • (1992) Microbiol. Rev , vol.56 , pp. 430-481
    • Young, R.1
  • 39
    • 0027475082 scopus 로고
    • Packing and hydrophobicity effects on protein folding and stability: effects of β-branched amino acids, valine and isoleucine, on the formation and stability of twostranded α-helical coiled coils/leucine zippers
    • Zhu, B. Y., M. E. Zhou, C. M. Kay, and R. S. Hodges, 1993 Packing and hydrophobicity effects on protein folding and stability: effects of β-branched amino acids, valine and isoleucine, on the formation and stability of twostranded α-helical coiled coils/leucine zippers. Protein Sci. 2(3): 383-394.
    • (1993) Protein Sci , vol.2 , Issue.3 , pp. 383-394
    • Zhu, B.Y.1    Zhou, M.E.2    Kay, C.M.3    Hodges, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.