메뉴 건너뛰기




Volumn 291, Issue 1, 2016, Pages 215-226

Structural plasticity of the protein plug that traps newly packaged genomes in podoviridae virions

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIOPHAGES; CIRCULAR DICHROISM SPECTROSCOPY; CONFORMATIONS; CRYSTALLOGRAPHY; DICHROISM; FILTRATION; GEL PERMEATION CHROMATOGRAPHY; GENES; MASS SPECTROMETRY; MEDICAL IMAGING; NEEDLES; OLIGOMERS; PH; PLASTICITY; VIRUSES;

EID: 84952946422     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.696260     Document Type: Article
Times cited : (14)

References (53)
  • 1
    • 0038392706 scopus 로고    scopus 로고
    • Bacteriophage observations and evolution
    • Ackermann, H. W. (2003) Bacteriophage observations and evolution. Res. Microbiol. 154, 245-251
    • (2003) Res. Microbiol , vol.154 , pp. 245-251
    • Ackermann, H.W.1
  • 2
    • 84887580353 scopus 로고    scopus 로고
    • Architecture of viral genome-delivery molecular machines
    • Bhardwaj, A., Olia, A. S., and Cingolani, G. (2014) Architecture of viral genome-delivery molecular machines. Curr. Opin. Struct. Biol. 25, 1-8
    • (2014) Curr. Opin. Struct. Biol , vol.25 , pp. 1-8
    • Bhardwaj, A.1    Olia, A.S.2    Cingolani, G.3
  • 3
    • 77952310806 scopus 로고    scopus 로고
    • "Let the phage do the work": Using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants
    • Teschke, C. M., and Parent, K. N. (2010) "Let the phage do the work": using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants. Virology 401, 119-130
    • (2010) Virology , vol.401 , pp. 119-130
    • Teschke, C.M.1    Parent, K.N.2
  • 4
    • 21844456877 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacteriophage P22 tail machine
    • Tang, L., Marion, W. R., Cingolani, G., Prevelige, P. E., and Johnson, J. E. (2005) Three-dimensional structure of the bacteriophage P22 tail machine. EMBO J. 24, 2087-2095
    • (2005) EMBO J , vol.24 , pp. 2087-2095
    • Tang, L.1    Marion, W.R.2    Cingolani, G.3    Prevelige, P.E.4    Johnson, J.E.5
  • 5
    • 66349109579 scopus 로고    scopus 로고
    • The P22 tail machine at subnanometer resolution reveals the architecture of an infection conduit
    • Lander, G. C., Khayat, R., Li, R., Prevelige, P. E., Potter, C. S., Carragher, B., and Johnson, J. E. (2009) The P22 tail machine at subnanometer resolution reveals the architecture of an infection conduit. Structure 17, 789-799
    • (2009) Structure , vol.17 , pp. 789-799
    • Lander, G.C.1    Khayat, R.2    Li, R.3    Prevelige, P.E.4    Potter, C.S.5    Carragher, B.6    Johnson, J.E.7
  • 7
    • 33744811672 scopus 로고    scopus 로고
    • Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery
    • Chang, J., Weigele, P., King, J., Chiu, W., and Jiang, W. (2006) Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery. Structure 14, 1073-1082
    • (2006) Structure , vol.14 , pp. 1073-1082
    • Chang, J.1    Weigele, P.2    King, J.3    Chiu, W.4    Jiang, W.5
  • 9
    • 0018160959 scopus 로고
    • A model for the adsorption of phage P22 to Salmonella typhimurium
    • Israel, V. (1978) A model for the adsorption of phage P22 to Salmonella typhimurium. J. Gen. Virol. 40, 669-673
    • (1978) J. Gen. Virol , vol.40 , pp. 669-673
    • Israel, V.1
  • 10
    • 0018842562 scopus 로고
    • Structure and functions of the bacteriophage P22 tail protein
    • Berget, P. B., and Poteete, A. R. (1980) Structure and functions of the bacteriophage P22 tail protein. J. Virol. 34, 234-243
    • (1980) J. Virol , vol.34 , pp. 234-243
    • Berget, P.B.1    Poteete, A.R.2
  • 12
    • 36849043686 scopus 로고    scopus 로고
    • Structure of phage P22 cell envelope-penetrating needle
    • Olia, A. S., Casjens, S., and Cingolani, G. (2007) Structure of phage P22 cell envelope-penetrating needle. Nat. Struct. Mol. Biol. 14, 1221-1226
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 1221-1226
    • Olia, A.S.1    Casjens, S.2    Cingolani, G.3
  • 13
    • 61449223647 scopus 로고    scopus 로고
    • Structural plasticity of the phage P22 tail needle gp26 probed with xenon gas
    • Olia, A. S., Casjens, S., and Cingolani, G. (2009) Structural plasticity of the phage P22 tail needle gp26 probed with xenon gas. Protein Sci. 18, 537-548
    • (2009) Protein Sci , vol.18 , pp. 537-548
    • Olia, A.S.1    Casjens, S.2    Cingolani, G.3
  • 14
    • 84894127143 scopus 로고    scopus 로고
    • Exploring the atomic structure and conformational flexibility of a 320 A long engineered viral fiber using x-ray crystallography
    • Bhardwaj, A., Casjens, S. R., and Cingolani, G. (2014) Exploring the atomic structure and conformational flexibility of a 320 A long engineered viral fiber using x-ray crystallography. Acta Crystallogr. D Biol. Crystallogr. 70, 342-353
    • (2014) Acta Crystallogr. D Biol. Crystallogr , vol.70 , pp. 342-353
    • Bhardwaj, A.1    Casjens, S.R.2    Cingolani, G.3
  • 15
    • 84876815569 scopus 로고    scopus 로고
    • Function and horizontal transfer of the small terminase subunit of the tailed bacteriophage Sf6 DNA packaging nanomotor
    • Leavitt, J. C., Gilcrease, E. B., Wilson, K., and Casjens, S. R. (2013) Function and horizontal transfer of the small terminase subunit of the tailed bacteriophage Sf6 DNA packaging nanomotor. Virology 440, 117-133
    • (2013) Virology , vol.440 , pp. 117-133
    • Leavitt, J.C.1    Gilcrease, E.B.2    Wilson, K.3    Casjens, S.R.4
  • 16
    • 67651085287 scopus 로고    scopus 로고
    • An evolutionarily conserved family of virion tail needles related to bacteriophage P22 gp26: Correlation between structural stability and length of the alpha-helical trimeric coiled coil
    • Bhardwaj, A., Walker-Kopp, N., Casjens, S. R., and Cingolani, G. (2009) An evolutionarily conserved family of virion tail needles related to bacteriophage P22 gp26: correlation between structural stability and length of the alpha-helical trimeric coiled coil. J. Mol. Biol. 391, 227-245
    • (2009) J. Mol. Biol , vol.391 , pp. 227-245
    • Bhardwaj, A.1    Walker-Kopp, N.2    Casjens, S.R.3    Cingolani, G.4
  • 17
    • 80052194652 scopus 로고    scopus 로고
    • Atomic structure of bacteriophage Sf6 tail needle knob
    • Bhardwaj, A., Molineux, I. J., Casjens, S. R., and Cingolani, G. (2011) Atomic structure of bacteriophage Sf6 tail needle knob. J. Biol. Chem. 286, 30867-30877
    • (2011) J. Biol. Chem , vol.286 , pp. 30867-30877
    • Bhardwaj, A.1    Molineux, I.J.2    Casjens, S.R.3    Cingolani, G.4
  • 18
    • 17044438215 scopus 로고    scopus 로고
    • The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture
    • Merckel, M. C., Huiskonen, J. T., Bamford, D. H., Goldman, A., and Tuma, R. (2005) The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture. Mol. Cell 18, 161-170
    • (2005) Mol. Cell , vol.18 , pp. 161-170
    • Merckel, M.C.1    Huiskonen, J.T.2    Bamford, D.H.3    Goldman, A.4    Tuma, R.5
  • 19
    • 0033613385 scopus 로고    scopus 로고
    • A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein
    • van Raaij, M. J., Mitraki, A., Lavigne, G., and Cusack, S. (1999) A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein. Nature 401, 935-938
    • (1999) Nature , vol.401 , pp. 935-938
    • Van Raaij, M.J.1    Mitraki, A.2    Lavigne, G.3    Cusack, S.4
  • 20
    • 34447283819 scopus 로고    scopus 로고
    • Domain organization and polarity of tail needle GP26 in the portal vertex structure of bacteriophage P22
    • Bhardwaj, A., Olia, A. S., Walker-Kopp, N., and Cingolani, G. (2007) Domain organization and polarity of tail needle GP26 in the portal vertex structure of bacteriophage P22. J. Mol. Biol. 371, 374-387
    • (2007) J. Mol. Biol , vol.371 , pp. 374-387
    • Bhardwaj, A.1    Olia, A.S.2    Walker-Kopp, N.3    Cingolani, G.4
  • 21
    • 84864848769 scopus 로고    scopus 로고
    • Structure of p22 headful packaging nuclease
    • Roy, A., and Cingolani, G. (2012) Structure of p22 headful packaging nuclease. J. Biol. Chem. 287, 28196-28205
    • (2012) J. Biol. Chem , vol.287 , pp. 28196-28205
    • Roy, A.1    Cingolani, G.2
  • 22
    • 84864834137 scopus 로고    scopus 로고
    • Small terminase couples viralDNAbinding to genome-packaging ATPase activity
    • Roy, A., Bhardwaj, A., Datta, P., Lander, G. C., and Cingolani, G. (2012) Small terminase couples viralDNAbinding to genome-packaging ATPase activity. Structure 20, 1403-1413
    • (2012) Structure , vol.20 , pp. 1403-1413
    • Roy, A.1    Bhardwaj, A.2    Datta, P.3    Lander, G.C.4    Cingolani, G.5
  • 24
    • 0021329694 scopus 로고
    • Steps in the stabilization of newly packaged DNA during phage P22 morphogenesis
    • Strauss, H., and King, J. (1984) Steps in the stabilization of newly packaged DNA during phage P22 morphogenesis. J. Mol. Biol. 172, 523-543
    • (1984) J. Mol. Biol , vol.172 , pp. 523-543
    • Strauss, H.1    King, J.2
  • 25
    • 85027920272 scopus 로고    scopus 로고
    • Three-dimensional structure of a viral genome-delivery portal vertex
    • Olia, A. S., Prevelige, P. E., Jr., Johnson, J. E., and Cingolani, G. (2011) Three-dimensional structure of a viral genome-delivery portal vertex. Nat. Struct. Mol. Biol. 18, 597-603
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 597-603
    • Olia, A.S.1    Prevelige, P.E.2    Johnson, J.E.3    Cingolani, G.4
  • 26
    • 34547616468 scopus 로고    scopus 로고
    • Role of gene 10 protein in the hierarchical assembly of the bacteriophage P22 portal vertex structure
    • Olia, A. S., Bhardwaj, A., Joss, L., Casjens, S., and Cingolani, G. (2007) Role of gene 10 protein in the hierarchical assembly of the bacteriophage P22 portal vertex structure. Biochemistry 46, 8776-8784
    • (2007) Biochemistry , vol.46 , pp. 8776-8784
    • Olia, A.S.1    Bhardwaj, A.2    Joss, L.3    Casjens, S.4    Cingolani, G.5
  • 27
    • 33748934964 scopus 로고    scopus 로고
    • Binding-induced stabilization and assembly of the phage P22 tail accessory factor gp4
    • Olia, A. S., Al-Bassam, J., Winn-Stapley, D. A., Joss, L., Casjens, S. R., and Cingolani, G. (2006) Binding-induced stabilization and assembly of the phage P22 tail accessory factor gp4. J. Mol. Biol. 363, 558-576
    • (2006) J. Mol. Biol , vol.363 , pp. 558-576
    • Olia, A.S.1    Al-Bassam, J.2    Winn-Stapley, D.A.3    Joss, L.4    Casjens, S.R.5    Cingolani, G.6
  • 28
    • 0017746030 scopus 로고
    • E proteins of bacteriophage P22: I. Identification and ejection from wild-type and defective particles
    • Israel, V. (1977) E proteins of bacteriophage P22: I. identification and ejection from wild-type and defective particles. J. Virol. 23, 91-97
    • (1977) J. Virol , vol.23 , pp. 91-97
    • Israel, V.1
  • 30
    • 78449253110 scopus 로고    scopus 로고
    • Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitro
    • Andres, D., Hanke, C., Baxa, U., Seul, A., Barbirz, S., and Seckler, R. (2010) Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitro. J. Biol. Chem. 285, 36768-36775
    • (2010) J. Biol. Chem , vol.285 , pp. 36768-36775
    • Andres, D.1    Hanke, C.2    Baxa, U.3    Seul, A.4    Barbirz, S.5    Seckler, R.6
  • 32
    • 0031570687 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain
    • Tao, Y., Strelkov, S. V., Mesyanzhinov, V. V., and Rossmann, M. G. (1997) Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure 5, 789-798
    • (1997) Structure , vol.5 , pp. 789-798
    • Tao, Y.1    Strelkov, S.V.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4
  • 34
    • 0034634450 scopus 로고    scopus 로고
    • Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association
    • Cingolani, G., Lashuel, H. A., Gerace, L., and Müller, C. W. (2000) Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association. FEBS Lett. 484, 291-298
    • (2000) FEBS Lett , vol.484 , pp. 291-298
    • Cingolani, G.1    Lashuel, H.A.2    Gerace, L.3    Müller, C.W.4
  • 35
    • 84873371088 scopus 로고    scopus 로고
    • Atomic structure of dual-specificity phosphatase 26, a novel p53 phosphatase
    • Lokareddy, R. K., Bhardwaj, A., and Cingolani, G. (2013) Atomic structure of dual-specificity phosphatase 26, a novel p53 phosphatase. Biochemistry 52, 938-948
    • (2013) Biochemistry , vol.52 , pp. 938-948
    • Lokareddy, R.K.1    Bhardwaj, A.2    Cingolani, G.3
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A. J. (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 63, 32-41
    • (2007) Acta Crystallogr. D Biol. Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 40
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 41
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 45
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725-738
    • (2010) Nat. Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 46
    • 84858751288 scopus 로고    scopus 로고
    • Structural evolution of the P22-like phages: Comparison of Sf6 and P22 procapsid and virion architectures
    • Parent, K. N., Gilcrease, E. B., Casjens, S. R., and Baker, T. S. (2012) Structural evolution of the P22-like phages: comparison of Sf6 and P22 procapsid and virion architectures. Virology 427, 177-188
    • (2012) Virology , vol.427 , pp. 177-188
    • Parent, K.N.1    Gilcrease, E.B.2    Casjens, S.R.3    Baker, T.S.4
  • 48
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., and Leith, A. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199
    • (1996) J. Struct. Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 49
    • 0035943385 scopus 로고    scopus 로고
    • Nucleotide sequence of coliphage HK620 and the evolution of lambdoid phages
    • Clark, A. J., Inwood, W., Cloutier, T., and Dhillon, T. S. (2001) Nucleotide sequence of coliphage HK620 and the evolution of lambdoid phages. J. Mol. Biol. 311, 657-679
    • (2001) J. Mol. Biol , vol.311 , pp. 657-679
    • Clark, A.J.1    Inwood, W.2    Cloutier, T.3    Dhillon, T.S.4
  • 50
    • 0017581778 scopus 로고
    • Functions of two new genes in Salmonella phage P22 assembly
    • Poteete, A. R., and King, J. (1977) Functions of two new genes in Salmonella phage P22 assembly. Virology 76, 725-739
    • (1977) Virology , vol.76 , pp. 725-739
    • Poteete, A.R.1    King, J.2
  • 51
    • 79952072125 scopus 로고    scopus 로고
    • Evolution of mosaically related tailed bacteriophage genomes seen through the lens of phage P22 virion assembly
    • Casjens, S. R., and Thuman-Commike, P. A. (2011) Evolution of mosaically related tailed bacteriophage genomes seen through the lens of phage P22 virion assembly. Virology 411, 393-415
    • (2011) Virology , vol.411 , pp. 393-415
    • Casjens, S.R.1    Thuman-Commike, P.A.2
  • 52
    • 0020361477 scopus 로고
    • Stoichiometry of the H-ATPase of growing and resting, aerobic Escherichia coli
    • Kashket, E. R. (1982) Stoichiometry of the H-ATPase of growing and resting, aerobic Escherichia coli. Biochemistry 21, 5534-5538
    • (1982) Biochemistry , vol.21 , pp. 5534-5538
    • Kashket, E.R.1
  • 53
    • 79958858245 scopus 로고    scopus 로고
    • Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation
    • Cingolani, G., and Duncan, T. M. (2011) Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation. Nat. Struct. Mol. Biol. 18, 701-707
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 701-707
    • Cingolani, G.1    Duncan, T.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.