메뉴 건너뛰기




Volumn 21, Issue 6, 2012, Pages 809-818

The protein gp74 from the bacteriophage HK97 functions as a HNH endonuclease

Author keywords

Bacteriophage HK97; Divalent metals; DNA digestion; HNH endonucleases; Zn 2+ finger

Indexed keywords

DNA; ENDONUCLEASE; PROTEIN; PROTEIN GP74; TRYPTOPHAN; UNCLASSIFIED DRUG; ZINC ION;

EID: 84861427386     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2064     Document Type: Article
Times cited : (30)

References (42)
  • 1
    • 0034716946 scopus 로고    scopus 로고
    • Genomic sequences of bacteriophages HK97 and HK022: Pervasive genetic mosaicism in the lambdoid bacteriophages
    • Juhala RJ, Ford ME, Duda RL, Youlton A, Hatfull GF, Hendrix RW (2000) Genomic sequences of bacteriophages HK97 and HK022: pervasive genetic mosaicism in the lambdoid bacteriophages. J Mol Biol 299:27-51
    • (2000) J Mol Biol , vol.299 , pp. 27-51
    • Juhala, R.J.1    Ford, M.E.2    Duda, R.L.3    Youlton, A.4    Hatfull, G.F.5    Hendrix, R.W.6
  • 3
    • 0029871788 scopus 로고    scopus 로고
    • Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82
    • DOI 10.1006/jmbi.1996.0185
    • Mahdi AA, Sharples GJ, Mandal TN, Lloyd RG (1996) Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82. J Mol Biol 257:561-573 (Pubitemid 26107222)
    • (1996) Journal of Molecular Biology , vol.257 , Issue.3 , pp. 561-573
    • Mahdi, A.A.1    Sharples, G.J.2    Mandal, T.N.3    Lloyd, R.G.4
  • 4
    • 0029020763 scopus 로고
    • S gene expression and the timing of lysis by bacteriophage lambda
    • Chang CY, Nam K, Young R (1995) S gene expression and the timing of lysis by bacteriophage lambda. J Bacteriol 177:3283-3294
    • (1995) J Bacteriol , vol.177 , pp. 3283-3294
    • Chang, C.Y.1    Nam, K.2    Young, R.3
  • 5
    • 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
  • 6
    • 0029097918 scopus 로고
    • Holins: Form and function in bacteriophage lysis
    • Young R, Blasi U (1995) Holins: form and function in bacteriophage lysis. FEMS Microbiol Rev 17:191-205
    • (1995) FEMS Microbiol Rev , vol.17 , pp. 191-205
    • Young, R.1    Blasi, U.2
  • 7
    • 0018613090 scopus 로고
    • A comprehensive molecular map of bacteriophage lambda
    • DOI 10.1016/0378-1119(79)90047-7
    • Szybalski EH, Szybalski W (1979) A comprehensive molecular map of bacteriophage lambda. Gene 7: 217-270 (Pubitemid 10195586)
    • (1979) Gene , vol.7 , Issue.3-4 , pp. 217-270
    • Szybalski, E.H.1    Szybalski, W.2
  • 10
    • 33644756595 scopus 로고    scopus 로고
    • Homing endonuclease structure and function
    • Stoddard BL (2005) Homing endonuclease structure and function. Q Rev Biophys 38:49-95
    • (2005) Q Rev Biophys , vol.38 , pp. 49-95
    • Stoddard, B.L.1
  • 11
    • 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 186:4307-4314 (Pubitemid 38802579)
    • (2004) Journal of Bacteriology , vol.186 , Issue.13 , pp. 4307-4314
    • Landthaler, M.1    Lau, N.C.2    Shub, D.A.3
  • 12
    • 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 137:91-100
    • (1991) J Gen Microbiol , vol.137 , pp. 91-100
    • Chak, K.F.1    Kuo, W.S.2    Lu, F.M.3    James, R.4
  • 13
    • 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 334:387-392 (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
  • 14
    • 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: 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
  • 15
    • 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 32:6129-6135 (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
  • 17
    • 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 37:3799-3810
    • (2009) Nucleic Acids Res , vol.37 , pp. 3799-3810
    • Sokolowska, M.1    Czapinska, H.2    Bochtler, M.3
  • 18
    • 4143108003 scopus 로고    scopus 로고
    • DNA binding and cleavage by the HNH homing endonuclease I-HmuI
    • DOI 10.1016/j.jmb.2004.07.032, PII S0022283604008599
    • Shen BW, Landthaler M, Shub DA, Stoddard BL (2004) DNA binding and cleavage by the HNH homing endonuclease I-HmuI. J Mol Biol 342:43-56 (Pubitemid 39094504)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.1 , pp. 43-56
    • Shen, B.W.1    Landthaler, M.2    Shub, D.A.3    Stoddard, B.L.4
  • 19
    • 0036440979 scopus 로고    scopus 로고
    • The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to double-stranded DNA by the H-N-H endonucleases
    • DOI 10.1016/S0022-2836(02)01092-6
    • Cheng YS, Hsia KC, Doudeva LG, Chak KF, Yuan HS (2002) The crystal structure of the nuclease domain of colicin E7 suggests a mechanism for binding to doublestranded DNA by the H-N-H endonucleases. J Mol Biol 324:227-236 (Pubitemid 35379023)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.2 , pp. 227-236
    • Cheng, Y.-S.1    Hsia, K.-C.2    Doudeva, L.G.3    Chak, K.-F.4    Yuan, H.S.5
  • 20
    • 33846895418 scopus 로고    scopus 로고
    • Structural basis for sequence-dependent DNA cleavage by nonspecific endonucleases
    • DOI 10.1093/nar/gkl621
    • Wang YT, Yang WJ, Li CL, Doudeva LG, Yuan HS (2007) Structural basis for sequence-dependent DNA cleavage by nonspecific endonucleases. Nucleic Acids Res 35:584-594 (Pubitemid 46232074)
    • (2007) Nucleic Acids Research , vol.35 , Issue.2 , pp. 584-594
    • Wang, Y.-T.1    Yang, W.-J.2    Li, C.-L.3    Doudeva, L.G.4    Yuan, H.S.5
  • 21
    • 34047123641 scopus 로고    scopus 로고
    • The Conserved Asparagine in the HNH Motif Serves an Important Structural Role in Metal Finger Endonucleases
    • DOI 10.1016/j.jmb.2007.02.044, PII S0022283607002252
    • Huang H, Yuan HS (2007) The conserved asparagine in the HNH motif serves an important structural role in metal finger endonucleases. J Mol Biol 368:812-821 (Pubitemid 46527620)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.3 , pp. 812-821
    • Huang, H.1    Yuan, H.S.2
  • 23
    • 4544287623 scopus 로고    scopus 로고
    • Structure-based analysis of the metal-dependent mechanism of H-N-H endonucleases
    • DOI 10.1074/jbc.M403719200
    • Mate MJ, Kleanthous C (2004) Structure-based analysis of the metal-dependent mechanism of H-N-H endonucleases. J Biol Chem 279:34763-34769 (Pubitemid 39318108)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34763-34769
    • Mate, M.J.1    Kleanthous, C.2
  • 24
    • 0030054233 scopus 로고    scopus 로고
    • Beyond homing: Competition between intron endonucleases confers a selective advantage on flanking genetic markers
    • DOI 10.1016/S0092-8674(00)80976-9
    • Goodrich-Blair H, Shub DA (1996) Beyond homing: competition between intron endonucleases confers a selective advantage on flanking genetic markers. Cell 84:211-221 (Pubitemid 26040841)
    • (1996) Cell , vol.84 , Issue.2 , pp. 211-221
    • Goodrich-Blair, H.1    Shub, D.A.2
  • 25
    • 75349114910 scopus 로고    scopus 로고
    • Phage T4 mobE promotes trans homing of the defunct homing endonuclease ITevIII
    • Wilson GW, Edgell DR (2009) Phage T4 mobE promotes trans homing of the defunct homing endonuclease ITevIII. Nucleic Acids Res 37:7110-7123
    • (2009) Nucleic Acids Res , vol.37 , pp. 7110-7123
    • Wilson, G.W.1    Edgell, D.R.2
  • 26
    • 0347994100 scopus 로고    scopus 로고
    • HNH family subclassification leads to identification of commonality in the His-Me endonuclease superfamily
    • DOI 10.1110/ps.03115604
    • Mehta P, Katta K, Krishnaswamy S (2004) HNH family subclassification leads to identification of commonality in the His-Me endonuclease superfamily. Protein Sci 13:295-300 (Pubitemid 38021162)
    • (2004) Protein Science , vol.13 , Issue.1 , pp. 295-300
    • Mehta, P.1    Katta, K.2    Krishnaswamy, S.3
  • 27
    • 0036529553 scopus 로고    scopus 로고
    • The zinc ion in the HNH motif of the endonuclease domain of colicin E7 is not required for DNA binding but is essential for DNA hydrolysis
    • Ku WY, Liu YW, Hsu YC, Liao CC, Liang PH, Yuan HS, Chak KF (2002) The zinc ion in the HNH motif of the endonuclease domain of colicin E7 is not required for DNA binding but is essential for DNA hydrolysis. Nucleic Acids Res 30:1670-1678 (Pubitemid 34679743)
    • (2002) Nucleic Acids Research , vol.30 , Issue.7 , pp. 1670-1678
    • Ku, W.-Y.1    Liu, Y.-W.2    Hsu, Y.-C.3    Liao, C.-C.4    Liang, P.-H.5    Yuan, H.S.6    Chak, K.-F.7
  • 28
    • 0034668391 scopus 로고    scopus 로고
    • Biochemical characterization of I-CmoeI reveals that this H-N-H homing endonuclease shares functional similarities with H-N-H colicins
    • Drouin M, Lucas P, Otis C, Lemieux C, Turmel M (2000) Biochemical characterization of I-CmoeI reveals that this H-N-H homing endonuclease shares functional similarities with H-N-H colicins. Nucleic Acids Res 28:4566-4572
    • (2000) Nucleic Acids Res , vol.28 , pp. 4566-4572
    • Drouin, M.1    Lucas, P.2    Otis, C.3    Lemieux, C.4    Turmel, M.5
  • 29
    • 0033559601 scopus 로고    scopus 로고
    • X-ray structure of T4 endonuclease VII: A DNA junction resolvase with a novel fold and unusual domain-swapped dimer architecture
    • Raaijmakers H, Vix O, Toro I, Golz S, Kemper B, Suck D (1999) X-ray structure of T4 endonuclease VII: a DNA junction resolvase with a novel fold and unusual domain-swapped dimer architecture. EMBO J 18: 1447-1458 (Pubitemid 29127059)
    • (1999) EMBO Journal , vol.18 , Issue.6 , pp. 1447-1458
    • Raaijmakers, H.1    Vix, O.2    Toro, I.3    Golz, S.4    Kemper, B.5    Suck, D.6
  • 31
    • 40449114454 scopus 로고    scopus 로고
    • Metals in proteins: Correlation between the metal-ion type, coordination number and the amino-acid residues involved in the coordination
    • DOI 10.1107/S090744490706595X, PII S090744490706595X
    • Dokmanic I, Sikic M, Tomic S (2008) Metals in proteins: correlation between the metal-ion type, coordination number and the amino-acid residues involved in the coordination. Acta Cryst D64:257-263. (Pubitemid 351348051)
    • (2008) Acta Crystallographica Section D: Biological Crystallography , vol.64 , Issue.3 , pp. 257-263
    • Dokmanic, I.1    Sikic, M.2    Tomic, S.3
  • 32
    • 0038452402 scopus 로고    scopus 로고
    • Coordination geometries of selected transition metal ions (Co2+, Ni2+, Cu2+, Zn2+, Cd2+, and Hg2+) in metalloproteins
    • Rulisek L, Vondrasek J (1998) Coordination geometries of selected transition metal ions (Co2+, Ni2+, Cu2+, Zn2+, Cd2+, and Hg2+) in metalloproteins. J Inorg Biochem 71:115-127
    • (1998) J Inorg Biochem , vol.71 , pp. 115-127
    • Rulisek, L.1    Vondrasek, J.2
  • 33
    • 0037439997 scopus 로고    scopus 로고
    • Structural classification of zinc fingers
    • DOI 10.1093/nar/gkg161
    • Krishna SS, Majumdar I, Grishin NV (2003) Structural classification of zinc fingers: survey and summary. Nucleic Acids Res 31:532-550 (Pubitemid 36175942)
    • (2003) Nucleic Acids Research , vol.31 , Issue.2 , pp. 532-550
    • Krishna, S.S.1    Majumdar, I.2    Grishin, N.V.3
  • 34
    • 34250358629 scopus 로고    scopus 로고
    • 2+
    • DOI 10.1093/nar/gkm114
    • Saravanan M, Vasu K, Kanakaraj R, Rao DN, Nagaraja V (2007) R.KpnI, an HNH superfamily REase, exhibits differential discrimination at non-canonical sequences in the presence of Ca2+ and Mg2+. Nucleic Acids Res 35:2777-2786 (Pubitemid 47073688)
    • (2007) Nucleic Acids Research , vol.35 , Issue.8 , pp. 2777-2786
    • Saravanan, M.1    Vasu, K.2    Kanakaraj, R.3    Rao, D.N.4    Nagaraja, V.5
  • 35
    • 79953139633 scopus 로고    scopus 로고
    • Creating directed doublestrand breaks with the Ref protein: A novel RecA-dependent nuclease from bacteriophage P1
    • Gruenig MC, Lu D, Won SJ, Dulberger CL, Manlick AJ, Keck JL, Cox MM (2011) Creating directed doublestrand breaks with the Ref protein: a novel RecA-dependent nuclease from bacteriophage P1. J Biol Chem 286:8240-8251
    • (2011) J Biol Chem , vol.286 , pp. 8240-8251
    • Gruenig, M.C.1    Lu, D.2    Won, S.J.3    Dulberger, C.L.4    Manlick, A.J.5    Keck, J.L.6    Cox, M.M.7
  • 36
    • 0036229271 scopus 로고    scopus 로고
    • Sequence analysis of the lactococcal bacteriophage bIL170: Insights into structural proteins and HNH endonucleases in dairy phages
    • Crutz-Le Coq AM, Cesselin B, Commissaire J, Anba J (2002) Sequence analysis of the lactococcal bacteriophage bIL170: insights into structural proteins and HNH endonucleases in dairy phages. Microbiology 148:985-1001 (Pubitemid 34436775)
    • (2002) Microbiology , vol.148 , Issue.4 , pp. 985-1001
    • Crutz-Le, C.A.-M.1    Cesselin, B.2    Commissaire, J.3    Anba, J.4
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411-2423
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 42
    • 0027936659 scopus 로고
    • Characterization of the interaction of natural proline-rich peptides with five different SH3 domains
    • Viguera AR, Arrondo JL, Musacchio A, Saraste M, Serrano L (1994) Characterization of the interaction of natural proline-rich peptides with five different SH3 domains. Biochemistry 33:10925-10933 (Pubitemid 24296346)
    • (1994) Biochemistry , vol.33 , Issue.36 , pp. 10925-10933
    • Viguera, A.R.1    Arrondo, J.L.R.2    Musacchio, A.3    Saraste, M.4    Serrano, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.