메뉴 건너뛰기




Volumn 15, Issue 2, 2004, Pages 233-244

The cytomegalovirus DNA polymerase subunit UL44 forms a C clamp-shaped dimer

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; MONOMER; PROTEIN DERIVATIVE; PROTEIN SUBUNIT; VIRUS PROTEIN;

EID: 3242688965     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.06.018     Document Type: Article
Times cited : (90)

References (48)
  • 1
    • 0030426254 scopus 로고    scopus 로고
    • The human cytomegalovirus genes and proteins required for DNA synthesis
    • Anders D.G., McCue L.A. The human cytomegalovirus genes and proteins required for DNA synthesis. Intervirology. 39:1996;378-388
    • (1996) Intervirology , vol.39 , pp. 378-388
    • Anders, D.G.1    McCue, L.A.2
  • 2
    • 0035038393 scopus 로고    scopus 로고
    • Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches
    • Bridges K.G., Chow C.S., Coen D.M. Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches. J. Virol. 75:2001;4990-4998
    • (2001) J. Virol. , vol.75 , pp. 4990-4998
    • Bridges, K.G.1    Chow, C.S.2    Coen, D.M.3
  • 3
    • 0035101674 scopus 로고    scopus 로고
    • Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer
    • Carrodeguas J.A., Theis K., Bogenhagen D.F., Kisker C. Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer. Mol. Cell. 7:2001;43-54
    • (2001) Mol. Cell , vol.7 , pp. 43-54
    • Carrodeguas, J.A.1    Theis, K.2    Bogenhagen, D.F.3    Kisker, C.4
  • 5
    • 3142544271 scopus 로고    scopus 로고
    • Human Kaposi's sarcoma herpesvirus processivity factor-8 functions as a dimer in DNA synthesis
    • Chen X., Lin K., Ricciardi R.P. Human Kaposi's sarcoma herpesvirus processivity factor-8 functions as a dimer in DNA synthesis. J. Biol. Chem. 279:2004;28375-28386
    • (2004) J. Biol. Chem. , vol.279 , pp. 28375-28386
    • Chen, X.1    Lin, K.2    Ricciardi, R.P.3
  • 6
    • 0028826076 scopus 로고
    • Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42
    • Chow C.S., Coen D.M. Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42. J. Virol. 69:1995;6965-6971
    • (1995) J. Virol. , vol.69 , pp. 6965-6971
    • Chow, C.S.1    Coen, D.M.2
  • 7
    • 0024793120 scopus 로고
    • Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5′ - 3′ exonuclease with ribonuclease H activity
    • Crute J.J., Lehman I.R. Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5′ - 3′ exonuclease with ribonuclease H activity. J. Biol. Chem. 264:1989;19266-19270
    • (1989) J. Biol. Chem. , vol.264 , pp. 19266-19270
    • Crute, J.J.1    Lehman, I.R.2
  • 8
    • 0027410405 scopus 로고
    • Functional analysis of the herpes simplex virus UL42 protein
    • Digard P., Chow C.S., Pirrit L., Coen D.M. Functional analysis of the herpes simplex virus UL42 protein. J. Virol. 67:1993;1159-1168
    • (1993) J. Virol. , vol.67 , pp. 1159-1168
    • Digard, P.1    Chow, C.S.2    Pirrit, L.3    Coen, D.M.4
  • 9
    • 0026636556 scopus 로고
    • Physical and functional interaction of human cytomegalovirus DNA polymerase and its accessory protein (ICP36) expressed in insect cells
    • Ertl P.F., Powell K.L. Physical and functional interaction of human cytomegalovirus DNA polymerase and its accessory protein (ICP36) expressed in insect cells. J. Virol. 66:1992;4126-4133
    • (1992) J. Virol. , vol.66 , pp. 4126-4133
    • Ertl, P.F.1    Powell, K.L.2
  • 10
    • 0023762811 scopus 로고
    • Purification of the herpes simplex virus type 1 65-kilodalton DNA-binding protein: Properties of the protein and evidence of its association with the virus-encoded DNA polymerase
    • Gallo M.L., Jackwood D.H., Murphy M., Marsden H.S., Parris D.S. Purification of the herpes simplex virus type 1 65-kilodalton DNA-binding protein. properties of the protein and evidence of its association with the virus-encoded DNA polymerase J. Virol. 62:1988;2874-2883
    • (1988) J. Virol. , vol.62 , pp. 2874-2883
    • Gallo, M.L.1    Jackwood, D.H.2    Murphy, M.3    Marsden, H.S.4    Parris, D.S.5
  • 11
    • 0024428273 scopus 로고
    • The essential 65-kilodalton DNA-binding protein of herpes simplex virus stimulates the virus-encoded DNA polymerase
    • Gallo M.L., Dorsky D.I., Crumpacker C.S., Parris D.S. The essential 65-kilodalton DNA-binding protein of herpes simplex virus stimulates the virus-encoded DNA polymerase. J. Virol. 63:1989;5023-5029
    • (1989) J. Virol. , vol.63 , pp. 5023-5029
    • Gallo, M.L.1    Dorsky, D.I.2    Crumpacker, C.S.3    Parris, D.S.4
  • 12
    • 0019489206 scopus 로고
    • Cytomegalovirus-infected cells contain a DNA-binding protein
    • Gibson W., Murphy T.L., Roby C. Cytomegalovirus-infected cells contain a DNA-binding protein. Virology. 111:1981;251-262
    • (1981) Virology , vol.111 , pp. 251-262
    • Gibson, W.1    Murphy, T.L.2    Roby, C.3
  • 13
    • 0028342556 scopus 로고
    • Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template
    • Gottlieb J., Challberg M.D. Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template. J. Virol. 68:1994;4937-4945
    • (1994) J. Virol. , vol.68 , pp. 4937-4945
    • Gottlieb, J.1    Challberg, M.D.2
  • 14
    • 0025253822 scopus 로고
    • The herpes simplex virus type 1 UL42 gene product: A subunit of DNA polymerase that functions to increase processivity
    • Gottlieb J., Marcy A.I., Coen D.M., Challberg M.D. The herpes simplex virus type 1 UL42 gene product. a subunit of DNA polymerase that functions to increase processivity J. Virol. 64:1990;5976-5987
    • (1990) J. Virol. , vol.64 , pp. 5976-5987
    • Gottlieb, J.1    Marcy, A.I.2    Coen, D.M.3    Challberg, M.D.4
  • 15
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J. Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. Cell. 87:1996;297-306
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 16
    • 0023239770 scopus 로고
    • Genomic localization, sequence analysis, and transcription of the putative human cytomegalovirus DNA polymerase gene
    • Heilbronn R., Jahn G., Burkle A., Freese U.K., Fleckenstein B., zur Hausen H. Genomic localization, sequence analysis, and transcription of the putative human cytomegalovirus DNA polymerase gene. J. Virol. 61:1987;119-124
    • (1987) J. Virol. , vol.61 , pp. 119-124
    • Heilbronn, R.1    Jahn, G.2    Burkle, A.3    Freese, U.K.4    Fleckenstein, B.5    Zur Hausen, H.6
  • 17
    • 0022999280 scopus 로고
    • Interaction of mutant thioredoxins of Escherichia coli with the gene 5 protein of phage T7. The redox capacity of thioredoxin is not required for stimulation of DNA polymerase activity
    • Huber H.E., Russel M., Model P., Richardson C.C. Interaction of mutant thioredoxins of Escherichia coli with the gene 5 protein of phage T7. The redox capacity of thioredoxin is not required for stimulation of DNA polymerase activity. J. Biol. Chem. 261:1986;15006-15012
    • (1986) J. Biol. Chem. , vol.261 , pp. 15006-15012
    • Huber, H.E.1    Russel, M.2    Model, P.3    Richardson, C.C.4
  • 18
    • 0028610526 scopus 로고
    • Intracellular localization and DNA-binding activity of a class of viral early phosphoproteins in human fibroblasts infected with human cytomegalovirus (Towne strain)
    • Iwayama S., Yamamoto T., Furuya T., Kobayashi R., Ikuta K., Hirai K. Intracellular localization and DNA-binding activity of a class of viral early phosphoproteins in human fibroblasts infected with human cytomegalovirus (Towne strain). J. Gen. Virol. 75:1994;3309-3318
    • (1994) J. Gen. Virol. , vol.75 , pp. 3309-3318
    • Iwayama, S.1    Yamamoto, T.2    Furuya, T.3    Kobayashi, R.4    Ikuta, K.5    Hirai, K.6
  • 20
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong X.P., Onrust R., O'Donnell M., Kuriyan J. Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme. a sliding DNA clamp Cell. 69:1992;425-437
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 22
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna T.S., Kong X.P., Gary S., Burgers P.M., Kuriyan J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell. 79:1994;1233-1243
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 25
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence M.C., Colman P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234:1993;946-950
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 26
    • 0347626042 scopus 로고    scopus 로고
    • Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44
    • a
    • Loregian A., Appleton B.A., Hogle J.M., Coen D.M. Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44. J. Virol. 78:2004;158-167. a
    • (2004) J. Virol. , vol.78 , pp. 158-167
    • Loregian, A.1    Appleton, B.A.2    Hogle, J.M.3    Coen, D.M.4
  • 27
    • 3242681272 scopus 로고    scopus 로고
    • Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein, UL44, are crucial for interaction with the UL54 catalytic subunit
    • b
    • Loregian A., Appleton B.A., Hogle J.M., Coen D.M. Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein, UL44, are crucial for interaction with the UL54 catalytic subunit. J. Virol. in press:2004;. b
    • (2004) J. Virol.
    • Loregian, A.1    Appleton, B.A.2    Hogle, J.M.3    Coen, D.M.4
  • 28
    • 0034723152 scopus 로고    scopus 로고
    • DNA polymerase switching: I. Replication factor C displaces DNA polymerase alpha prior to PCNA loading
    • Maga G., Stucki M., Spadari S., Hubscher U. DNA polymerase switching. I. Replication factor C displaces DNA polymerase alpha prior to PCNA loading J. Mol. Biol. 295:2000;791-801
    • (2000) J. Mol. Biol. , vol.295 , pp. 791-801
    • Maga, G.1    Stucki, M.2    Spadari, S.3    Hubscher, U.4
  • 29
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics. 16:2000;404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 30
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:1999;156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 31
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D. photorealistic molecular graphics Methods Enzymol. 277:1997;505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 33
    • 0030070111 scopus 로고    scopus 로고
    • A molecular switch in a replication machine defined by an internal competition for protein rings
    • Naktinis V., Turner J., O'Donnell M. A molecular switch in a replication machine defined by an internal competition for protein rings. Cell. 84:1996;137-145
    • (1996) Cell , vol.84 , pp. 137-145
    • Naktinis, V.1    Turner, J.2    O'Donnell, M.3
  • 34
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 35
    • 0035958740 scopus 로고    scopus 로고
    • In silico structural and functional analysis of the human cytomegalovirus (HHV5) genome
    • Novotny J., Rigoutsos I., Coleman D., Shenk T. In silico structural and functional analysis of the human cytomegalovirus (HHV5) genome. J. Mol. Biol. 310:2001;1151-1166
    • (2001) J. Mol. Biol. , vol.310 , pp. 1151-1166
    • Novotny, J.1    Rigoutsos, I.2    Coleman, D.3    Shenk, T.4
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 0034753799 scopus 로고    scopus 로고
    • Linear diffusion on DNA despite high-affinity binding by a DNA polymerase processivity factor
    • Randell J.C., Coen D.M. Linear diffusion on DNA despite high-affinity binding by a DNA polymerase processivity factor. Mol. Cell. 8:2001;911-920
    • (2001) Mol. Cell , vol.8 , pp. 911-920
    • Randell, J.C.1    Coen, D.M.2
  • 38
    • 0347627532 scopus 로고    scopus 로고
    • The herpes simplex virus processivity factor, UL42, binds DNA as a monomer
    • Randell J.C., Coen D.M. The herpes simplex virus processivity factor, UL42, binds DNA as a monomer. J. Mol. Biol. 335:2004;409-413
    • (2004) J. Mol. Biol. , vol.335 , pp. 409-413
    • Randell, J.C.1    Coen, D.M.2
  • 39
    • 0025809742 scopus 로고
    • Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme
    • Stukenberg P.T., Studwell-Vaughan P.S., O'Donnell M. Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 266:1991;11328-11334
    • (1991) J. Biol. Chem. , vol.266 , pp. 11328-11334
    • Stukenberg, P.T.1    Studwell-Vaughan, P.S.2    O'Donnell, M.3
  • 42
    • 0034734837 scopus 로고    scopus 로고
    • Analysis of in vitro activities of herpes simplex virus type 1 UL42 mutant proteins: Correlation with in vivo function
    • Thornton K.E., Chaudhuri M., Monahan S.J., Grinstead L.A., Parris D.S. Analysis of in vitro activities of herpes simplex virus type 1 UL42 mutant proteins. correlation with in vivo function Virology. 275:2000;373-390
    • (2000) Virology , vol.275 , pp. 373-390
    • Thornton, K.E.1    Chaudhuri, M.2    Monahan, S.J.3    Grinstead, L.A.4    Parris, D.S.5
  • 43
    • 0027448643 scopus 로고
    • Functional interaction between Epstein-Barr virus DNA polymerase catalytic subunit and its accessory subunit in vitro
    • Tsurumi T., Daikoku T., Kurachi R., Nishiyama Y. Functional interaction between Epstein-Barr virus DNA polymerase catalytic subunit and its accessory subunit in vitro. J. Virol. 67:1993;7648-7653
    • (1993) J. Virol. , vol.67 , pp. 7648-7653
    • Tsurumi, T.1    Daikoku, T.2    Kurachi, R.3    Nishiyama, Y.4
  • 44
  • 45
    • 0037523309 scopus 로고    scopus 로고
    • The diverse spectrum of sliding clamp interacting proteins
    • Vivona J.B., Kelman Z. The diverse spectrum of sliding clamp interacting proteins. FEBS Lett. 546:2003;167-172
    • (2003) FEBS Lett. , vol.546 , pp. 167-172
    • Vivona, J.B.1    Kelman, Z.2
  • 46
    • 0028153248 scopus 로고
    • Functional analysis of human cytomegalovirus polymerase accessory protein
    • Weiland K.L., Oien N.L., Homa F., Wathen M.W. Functional analysis of human cytomegalovirus polymerase accessory protein. Virus Res. 34:1994;191-206
    • (1994) Virus Res. , vol.34 , pp. 191-206
    • Weiland, K.L.1    Oien, N.L.2    Homa, F.3    Wathen, M.W.4
  • 47
    • 0032888971 scopus 로고    scopus 로고
    • Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate
    • Weisshart K., Chow C.S., Coen D.M. Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate. J. Virol. 73:1999;55-66
    • (1999) J. Virol. , vol.73 , pp. 55-66
    • Weisshart, K.1    Chow, C.S.2    Coen, D.M.3
  • 48
    • 0033867542 scopus 로고    scopus 로고
    • The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase
    • Zuccola H.J., Filman D.J., Coen D.M., Hogle J.M. The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase. Mol. Cell. 5:2000;267-278
    • (2000) Mol. Cell , vol.5 , pp. 267-278
    • Zuccola, H.J.1    Filman, D.J.2    Coen, D.M.3    Hogle, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.