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Volumn 111, Issue 16, 2014, Pages 6022-6027

HNH proteins are a widespread component of phage DNA packaging machines

Author keywords

Bacteriophage HK97; HNH endonuclease; Molecular chaperone

Indexed keywords

BACTERIAL PROTEIN; HNH PROTEIN; UNCLASSIFIED DRUG;

EID: 84899101737     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1320952111     Document Type: Article
Times cited : (103)

References (35)
  • 1
    • 84858273215 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging machine
    • Feiss M, Rao VB (2012) The bacteriophage DNA packaging machine. Adv Exp Med Biol 726:489-509.
    • (2012) Adv Exp Med Biol , vol.726 , pp. 489-509
    • Feiss, M.1    Rao, V.B.2
  • 2
    • 57649226492 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging motor
    • Rao VB, Feiss M (2008) The bacteriophage DNA packaging motor. Annu Rev Genet 42:647-681.
    • (2008) Annu Rev Genet , vol.42 , pp. 647-681
    • Rao, V.B.1    Feiss, M.2
  • 3
    • 0023474746 scopus 로고
    • A novel in vitro DNA packaging system demonstrating a direct role for the bacteriophage lambda FI gene product
    • Davidson A, Gold M (1987) A novel in vitro DNA packaging system demonstrating a direct role for the bacteriophage lambda FI gene product. Virology 161(2):305-314.
    • (1987) Virology , vol.161 , Issue.2 , pp. 305-314
    • Davidson, A.1    Gold, M.2
  • 4
    • 0023898550 scopus 로고
    • Bacteriophage lambda DNA packaging. The product of the FI gene promotes the incorporation of the prohead to the DNA-terminase complex
    • Becker A, Murialdo H, Lucko H, Morell J (1988) Bacteriophage lambda DNA packaging. The product of the FI gene promotes the incorporation of the prohead to the DNA-terminase complex. J Mol Biol 199(4):597-607.
    • (1988) J Mol Biol , vol.199 , Issue.4 , pp. 597-607
    • Becker, A.1    Murialdo, H.2    Lucko, H.3    Morell, J.4
  • 5
    • 0029117830 scopus 로고
    • Role of gpFI protein in DNA packaging by bacteriophage lambda
    • Catalano CE, Tomka MA (1995) Role of gpFI protein in DNA packaging by bacteriophage lambda. Biochemistry 34(31):10036-10042.
    • (1995) Biochemistry , vol.34 , Issue.31 , pp. 10036-10042
    • Catalano, C.E.1    Tomka, M.A.2
  • 6
    • 1942436909 scopus 로고    scopus 로고
    • Initial cos cleavage of bacteriophage lambda concatemers requires proheads and gpFI in in vivo
    • DOI 10.1111/j.1365-2958.2004.03990.x
    • Sippy J, Feiss M (2004) Initial cos cleavage of bacteriophage lambda concatemers requires proheads and gpFI in vivo. Mol Microbiol 52(2):501-513. (Pubitemid 38520718)
    • (2004) Molecular Microbiology , vol.52 , Issue.2 , pp. 501-513
    • Sippy, J.1    Feiss, M.2
  • 7
    • 84866419716 scopus 로고    scopus 로고
    • Structural and biochemical characterization of phage λ FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity
    • Popovic A, et al. (2012) Structural and biochemical characterization of phage λ FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity. J Biol Chem 287(38):32085-32095.
    • (2012) J Biol Chem , vol.287 , Issue.38 , pp. 32085-32095
    • Popovic, A.1
  • 8
    • 0023225629 scopus 로고
    • A small viral RNA is required for in vitro packaging of bacteriophage phi29 DNA
    • Guo PX, Erickson S, Anderson D (1987) A small viral RNA is required for in vitro packaging of bacteriophage phi 29 DNA. Science 236(4802):690-694. (Pubitemid 17076855)
    • (1987) Science , vol.236 , Issue.4802 , pp. 690-694
    • Guo, P.1    Erickson, S.2    Anderson, D.3
  • 9
    • 0033593367 scopus 로고    scopus 로고
    • Association of Holliday-structure resolving endonuclease VII with gp20 from the packaging machine of phage T4
    • DOI 10.1006/jmbi.1998.2399
    • Golz S, Kemper B (1999) Association of holliday-structure resolving endonuclease VII with gp20 from the packaging machine of phage T4. J Mol Biol 285(3):1131-1144. (Pubitemid 29054321)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.3 , pp. 1131-1144
    • Golz, S.1    Kemper, B.2
  • 10
    • 84861427386 scopus 로고    scopus 로고
    • The protein gp74 from the bacteriophage HK97 functions as a HNH endonuclease
    • Moodley S, Maxwell KL, Kanelis V (2012) The protein gp74 from the bacteriophage HK97 functions as a HNH endonuclease. Protein Sci 21(6):809-818.
    • (2012) Protein Sci , vol.21 , Issue.6 , pp. 809-818
    • Moodley, S.1    Maxwell, K.L.2    Kanelis, V.3
  • 11
    • 84858077472 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Punta M, et al. (2012) The Pfam protein families database. Nucleic Acids Res 40(Database issue):D290-D301.
    • (2012) Nucleic Acids Res , vol.40 , Issue.DATABASE ISSUE
    • Punta, M.1
  • 12
    • 33644756595 scopus 로고    scopus 로고
    • Homing endonuclease structure and function
    • Stoddard BL (2005) Homing endonuclease structure and function. Q Rev Biophys 38(1):49-95.
    • (2005) Q Rev Biophys , vol.38 , Issue.1 , pp. 49-95
    • Stoddard, B.L.1
  • 13
    • 3042606642 scopus 로고    scopus 로고
    • Group I intron homing in Bacillus phages SPO1 and SP82: A gene conversion event initiated by a nicking homing endonuclease
    • DOI 10.1128/JB.186.13.4307-4314.2004
    • Landthaler M, Lau NC, Shub DA (2004) Group I intron homing in Bacillus phages SPO1 and SP82: A gene conversion event initiated by a nicking homing endonuclease. J Bacteriol 186(13):4307-4314. (Pubitemid 38802579)
    • (2004) Journal of Bacteriology , vol.186 , Issue.13 , pp. 4307-4314
    • Landthaler, M.1    Lau, N.C.2    Shub, D.A.3
  • 14
    • 0025965595 scopus 로고
    • Cloning and characterization of the ColE7 plasmid
    • Chak KF, Kuo WS, Lu FM, James R (1991) Cloning and characterization of the ColE7 plasmid. J Gen Microbiol 137(1):91-100.
    • (1991) J Gen Microbiol , vol.137 , Issue.1 , pp. 91-100
    • Chak, K.F.1    Kuo, W.S.2    Lu, F.M.3    James, R.4
  • 15
    • 0032169937 scopus 로고    scopus 로고
    • Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli
    • Pommer AJ, Wallis R, Moore GR, James R, Kleanthous C (1998) Enzymological characterization of the nuclease domain from the bacterial toxin colicin E9 from Escherichia coli. Biochem J 334(Pt 2):387-392. (Pubitemid 28448581)
    • (1998) Biochemical Journal , vol.334 , Issue.2 , pp. 387-392
    • Pommer, A.J.1    Wallis, R.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 16
    • 0027155821 scopus 로고
    • Molecular structures and functions of pyocins S1 and S2 in Pseudomonas aeruginosa
    • Sano Y, Matsui H, Kobayashi M, Kageyama M (1993) Molecular structures and functions of pyocins S1 and S2 in Pseudomonas aeruginosa. J Bacteriol 175(10):2907-2916. (Pubitemid 23148723)
    • (1993) Journal of Bacteriology , vol.175 , Issue.10 , pp. 2907-2916
    • Sano, Y.1    Matsui, H.2    Kobayashi, M.3    Kageyama, M.4
  • 17
    • 11344267268 scopus 로고    scopus 로고
    • Type II restriction endonuclease R.Kpnl is a member of the HNH nuclease superfamily
    • DOI 10.1093/nar/gkh951
    • Saravanan M, Bujnicki JM, Cymerman IA, Rao DN, Nagaraja V (2004) Type II restriction endonuclease R.KpnI is a member of the HNH nuclease superfamily. Nucleic Acids Res 32(20):6129-6135. (Pubitemid 40074007)
    • (2004) Nucleic Acids Research , vol.32 , Issue.20 , pp. 6129-6135
    • Saravanan, M.1    Bujnicki, J.M.2    Cymerman, I.A.3    Rao, D.N.4    Nagaraja, V.5
  • 18
    • 77953604755 scopus 로고    scopus 로고
    • Unusual target site disruption by the rare-cutting HNH restriction endonuclease PacI
    • Shen BW, et al. (2010) Unusual target site disruption by the rare-cutting HNH restriction endonuclease PacI. Structure 18(6):734-743.
    • (2010) Structure , vol.18 , Issue.6 , pp. 734-743
    • Shen, B.W.1
  • 19
    • 67649888360 scopus 로고    scopus 로고
    • Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA
    • Sokolowska M, Czapinska H, Bochtler M (2009) Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA. Nucleic Acids Res 37(11):3799-3810.
    • (2009) Nucleic Acids Res , vol.37 , Issue.11 , pp. 3799-3810
    • Sokolowska, M.1    Czapinska, H.2    Bochtler, M.3
  • 20
    • 84871802688 scopus 로고    scopus 로고
    • Natural zinc ribbon HNH endonucleases and engineered zinc finger nicking endonuclease
    • Xu SY, Gupta YK (2013) Natural zinc ribbon HNH endonucleases and engineered zinc finger nicking endonuclease. Nucleic Acids Res 41(1):378-390.
    • (2013) Nucleic Acids Res , vol.41 , Issue.1 , pp. 378-390
    • Xu, S.Y.1    Gupta, Y.K.2
  • 21
    • 84879551382 scopus 로고    scopus 로고
    • A conserved spiral structure for highly diverged phage tail assembly chaperones
    • Pell LG, et al. (2013) A conserved spiral structure for highly diverged phage tail assembly chaperones. J Mol Biol 425(14):2436-2449.
    • (2013) J Mol Biol , vol.425 , Issue.14 , pp. 2436-2449
    • Pell, L.G.1
  • 22
    • 73849109239 scopus 로고    scopus 로고
    • The crystal structure of bacteriophage HK97 gp6: Defining a large family of head-tail connector proteins
    • Cardarelli L, et al. (2010) The crystal structure of bacteriophage HK97 gp6: Defining a large family of head-tail connector proteins. J Mol Biol 395(4):754-768.
    • (2010) J Mol Biol , vol.395 , Issue.4 , pp. 754-768
    • Cardarelli, L.1
  • 23
    • 0028969695 scopus 로고
    • Structural transitions during bacteriophage HK97 head assembly
    • Duda RL, et al. (1995) Structural transitions during bacteriophage HK97 head assembly. J Mol Biol 247(4):618-635.
    • (1995) J Mol Biol , vol.247 , Issue.4 , pp. 618-635
    • Duda, R.L.1
  • 24
    • 84879551382 scopus 로고    scopus 로고
    • A conserved spiral structure for highly diverged phage tail assembly chaperones
    • Pell LG, et al. (2013) A conserved spiral structure for highly diverged phage tail assembly chaperones. J Mol Biol 425(14):2436-2449.
    • (2013) J Mol Biol , vol.425 , Issue.14 , pp. 2436-2449
    • Pell, L.G.1
  • 25
    • 61849155151 scopus 로고    scopus 로고
    • The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system
    • Pell LG, Kanelis V, Donaldson LW, Howell PL, Davidson AR (2009) The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc Natl Acad Sci USA 106(11):4160-4165.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.11 , pp. 4160-4165
    • Pell, L.G.1    Kanelis, V.2    Donaldson, L.W.3    Howell, P.L.4    Davidson, A.R.5
  • 26
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: Interactive sequence similarity searching
    • Finn RD, Clements J, Eddy SR (2011) HMMER web server: Interactive sequence similarity searching. Nucleic Acids Res 39(Web Server issue):W29-37.
    • (2011) Nucleic Acids Res , vol.39 , Issue.WEB SERVER ISSUE
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 28
    • 0021100395 scopus 로고
    • The bacteriophage lambda terminase. Partial purification and preliminary characterization of properties
    • Gold M, Becker A (1983) The bacteriophage lambda terminase. Partial purification and preliminary characterization of properties. J Biol Chem 258(23):14619-14625.
    • (1983) J Biol Chem , vol.258 , Issue.23 , pp. 14619-14625
    • Gold, M.1    Becker, A.2
  • 29
    • 0018751698 scopus 로고
    • Purification and properties of proteins essential to DNA encapsulation by phage P22
    • DOI 10.1016/0042-6822(79)90509-9
    • Poteete AR, Botstein D (1979) Purification and properties of proteins essential to DNA encapsulation by phage P22. Virology 95(2):565-573. (Pubitemid 9199415)
    • (1979) Virology , vol.95 , Issue.2 , pp. 565-573
    • Poteete, A.R.1    Botstein, D.2
  • 30
    • 0021718056 scopus 로고
    • The maturation of coliphage lambda DNA in the absence of its packaging
    • DOI 10.1016/0378-1119(84)90119-7
    • Murialdo H, Fife WL (1984) The maturation of coliphage lambda DNA in the absence of its packaging. Gene 30(1-3):183-194. (Pubitemid 15201776)
    • (1984) Gene , vol.30 , Issue.1-3 , pp. 183-194
    • Murialdo, H.1    Fife, W.L.2
  • 32
    • 0028560406 scopus 로고
    • Chromosome end formation in phage lambda, catalyzed by terminase, is controlled by two DNA elements of cos, cosN and R3, and by ATP
    • Higgins RR, Becker A (1994) Chromosome end formation in phage lambda, catalyzed by terminase, is controlled by two DNA elements of cos, cosN and R3, and by ATP. EMBO J 13(24):6152-6161.
    • (1994) EMBO J , vol.13 , Issue.24 , pp. 6152-6161
    • Higgins, R.R.1    Becker, A.2
  • 33
    • 84866389227 scopus 로고    scopus 로고
    • The bacteriophage HK97 gp15 moron element encodes a novel superinfection exclusion protein
    • Cumby N, Edwards AM, Davidson AR, Maxwell KL (2012) The bacteriophage HK97 gp15 moron element encodes a novel superinfection exclusion protein. J Bacteriol 194(18):5012-5019.
    • (2012) J Bacteriol , vol.194 , Issue.18 , pp. 5012-5019
    • Cumby, N.1    Edwards, A.M.2    Davidson, A.R.3    Maxwell, K.L.4
  • 34
    • 84875619226 scopus 로고    scopus 로고
    • MAFFT multiple sequence alignment software version 7: Improvements in performance and usability
    • Katoh K, Standley DM (2013) MAFFT multiple sequence alignment software version 7: Improvements in performance and usability. Molecular Biology and Evolution 30: 772-780.
    • (2013) Molecular Biology and Evolution , vol.30 , pp. 772-780
    • Katoh, K.1    Standley, D.M.2
  • 35
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2 - A multiple sequence alignment editor and analysis workbench
    • Waterhouse AM, Procter JB, Martin DM, Clamp M, Barton GJ (2009) Jalview Version 2 - a multiple sequence alignment editor and analysis workbench. Bioinformatics 25(9):1189-1191.
    • (2009) Bioinformatics , vol.25 , Issue.9 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.