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Volumn 397, Issue 3, 2010, Pages 520-525

Kaposi's sarcoma-associated herpesvirus processivity factor-8 dimerizes in cytoplasm before being translocated to nucleus

Author keywords

Dimerization; Herpesvirus; KSHV; PF 8; Processivity factor

Indexed keywords

AMINO ACID; DIMER; DNA POLYMERASE; HOMODIMER; PROCESSIVITY FACTOR 8; UNCLASSIFIED DRUG;

EID: 77954218537     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.05.147     Document Type: Article
Times cited : (10)

References (32)
  • 4
    • 0029069445 scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas
    • Cesarman E., Chang Y., Moore P.S., Said J.W., Knowles D.M. Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas. N. Engl. J. Med. 1995, 332:1186-1191.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 1186-1191
    • Cesarman, E.1    Chang, Y.2    Moore, P.S.3    Said, J.W.4    Knowles, D.M.5
  • 6
    • 0029876473 scopus 로고    scopus 로고
    • Lytic growth of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) in culture
    • Renne R., Zhong W., Herndier B., McGrath M., Abbey N., Kedes D., Ganem D. Lytic growth of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) in culture. Nat. Med. 1996, 2:342-346.
    • (1996) Nat. Med. , vol.2 , pp. 342-346
    • Renne, R.1    Zhong, W.2    Herndier, B.3    McGrath, M.4    Abbey, N.5    Kedes, D.6    Ganem, D.7
  • 7
    • 10544237674 scopus 로고    scopus 로고
    • Selective switch between latency and lytic replication of Kaposi's sarcoma herpesvirus and Epstein-Barr virus in dually infected body cavity lymphoma cells
    • Miller G., Heston L., Grogan E., Gradoville L., Rigsby M., Sun R., Shedd D., Kushnaryov V.M., Grossberg S., Chang Y. Selective switch between latency and lytic replication of Kaposi's sarcoma herpesvirus and Epstein-Barr virus in dually infected body cavity lymphoma cells. J. Virol. 1997, 71:314-324.
    • (1997) J. Virol. , vol.71 , pp. 314-324
    • Miller, G.1    Heston, L.2    Grogan, E.3    Gradoville, L.4    Rigsby, M.5    Sun, R.6    Shedd, D.7    Kushnaryov, V.M.8    Grossberg, S.9    Chang, Y.10
  • 8
    • 0033597453 scopus 로고    scopus 로고
    • Efficient persistence of extrachromosomal KSHV DNA mediated by latency-associated nuclear antigen
    • Ballestas M.E., Chatis P.A., Kaye K.M. Efficient persistence of extrachromosomal KSHV DNA mediated by latency-associated nuclear antigen. Science 1999, 284:641-644.
    • (1999) Science , vol.284 , pp. 641-644
    • Ballestas, M.E.1    Chatis, P.A.2    Kaye, K.M.3
  • 9
    • 0034614893 scopus 로고    scopus 로고
    • Viral G protein-coupled receptor and Kaposi's sarcoma: a model of paracrine neoplasia?
    • Cesarman E., Mesri E.A., Gershengorn M.C. Viral G protein-coupled receptor and Kaposi's sarcoma: a model of paracrine neoplasia?. J. Exp. Med. 2000, 191:417-422.
    • (2000) J. Exp. Med. , vol.191 , pp. 417-422
    • Cesarman, E.1    Mesri, E.A.2    Gershengorn, M.C.3
  • 10
    • 1542571327 scopus 로고    scopus 로고
    • Inefficient establishment of KSHV latency suggests an additional role for continued lytic replication in Kaposi sarcoma pathogenesis
    • Grundhoff A., Ganem D. Inefficient establishment of KSHV latency suggests an additional role for continued lytic replication in Kaposi sarcoma pathogenesis. J. Clin. Invest. 2004, 113:124-136.
    • (2004) J. Clin. Invest. , vol.113 , pp. 124-136
    • Grundhoff, A.1    Ganem, D.2
  • 11
    • 0035152285 scopus 로고    scopus 로고
    • Origin-independent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the ORF-K8 protein and cellular PML
    • Wu F.Y., Ahn J.H., Alcendor D.J., Jang W.J., Xiao J., Hayward S.D., Hayward G.S. Origin-independent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the ORF-K8 protein and cellular PML. J. Virol. 2001, 75:1487-1506.
    • (2001) J. Virol. , vol.75 , pp. 1487-1506
    • Wu, F.Y.1    Ahn, J.H.2    Alcendor, D.J.3    Jang, W.J.4    Xiao, J.5    Hayward, S.D.6    Hayward, G.S.7
  • 12
    • 1242328736 scopus 로고    scopus 로고
    • Amplification of the Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 lytic origin of DNA replication is dependent upon a cis-acting AT-rich region and an ORF50 response element and the trans-acting factors ORF50 (K-Rta) and K8 (K-bZIP)
    • AuCoin D.P., Colletti K.S., Cei S.A., Papouskova I., Tarrant M., Pari G.S. Amplification of the Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 lytic origin of DNA replication is dependent upon a cis-acting AT-rich region and an ORF50 response element and the trans-acting factors ORF50 (K-Rta) and K8 (K-bZIP). Virology 2004, 318:542-555.
    • (2004) Virology , vol.318 , pp. 542-555
    • AuCoin, D.P.1    Colletti, K.S.2    Cei, S.A.3    Papouskova, I.4    Tarrant, M.5    Pari, G.S.6
  • 13
    • 0031776461 scopus 로고    scopus 로고
    • Cloning and functional analysis of Kaposi's sarcoma-associated herpesvirus DNA polymerase and its processivity factor
    • Lin K., Dai C.Y., Ricciardi R.P. Cloning and functional analysis of Kaposi's sarcoma-associated herpesvirus DNA polymerase and its processivity factor. J. Virol. 1998, 72:6228-6232.
    • (1998) J. Virol. , vol.72 , pp. 6228-6232
    • Lin, K.1    Dai, C.Y.2    Ricciardi, R.P.3
  • 14
    • 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. 2004, 279:28375-28386.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28375-28386
    • Chen, X.1    Lin, K.2    Ricciardi, R.P.3
  • 15
    • 3242688965 scopus 로고    scopus 로고
    • The cytomegalovirus DNA polymerase subunit UL44 forms a C clamp-shaped dimer
    • Appleton B.A., Loregian A., Filman D.J., Coen D.M., Hogle J.M. The cytomegalovirus DNA polymerase subunit UL44 forms a C clamp-shaped dimer. Mol. Cell 2004, 15:233-244.
    • (2004) Mol. Cell , vol.15 , pp. 233-244
    • Appleton, B.A.1    Loregian, A.2    Filman, D.J.3    Coen, D.M.4    Hogle, J.M.5
  • 17
    • 74049134918 scopus 로고    scopus 로고
    • Each monomer of the dimeric accessory protein for human mitochondrial DNA polymerase has a distinct role in conferring processivity
    • Lee Y.S., Lee S., Demeler B., Molineux I.J., Johnson K.A., Yin Y.W. Each monomer of the dimeric accessory protein for human mitochondrial DNA polymerase has a distinct role in conferring processivity. J. Biol. Chem. 2010, 285:1490-1499.
    • (2010) J. Biol. Chem. , vol.285 , pp. 1490-1499
    • Lee, Y.S.1    Lee, S.2    Demeler, B.3    Molineux, I.J.4    Johnson, K.A.5    Yin, Y.W.6
  • 18
    • 24944451474 scopus 로고    scopus 로고
    • Processivity factor of KSHV contains a nuclear localization signal and binding domains for transporting viral DNA polymerase into the nucleus
    • Chen Y., Ciustea M., Ricciardi R.P. Processivity factor of KSHV contains a nuclear localization signal and binding domains for transporting viral DNA polymerase into the nucleus. Virology 2005, 340:183-191.
    • (2005) Virology , vol.340 , pp. 183-191
    • Chen, Y.1    Ciustea, M.2    Ricciardi, R.P.3
  • 19
    • 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 1992, 69:425-437.
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 20
    • 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 1994, 79:1233-1243.
    • (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
  • 21
    • 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. 2004, 335:409-413.
    • (2004) J. Mol. Biol. , vol.335 , pp. 409-413
    • Randell, J.C.1    Coen, D.M.2
  • 23
    • 57349121130 scopus 로고    scopus 로고
    • Role of homodimerization of human cytomegalovirus DNA polymerase accessory protein UL44 in origin-dependent DNA replication in cells
    • Sinigalia E., Alvisi G., Mercorelli B., Coen D.M., Pari G.S., Jans D.A., Ripalti A., Palu G., Loregian A. Role of homodimerization of human cytomegalovirus DNA polymerase accessory protein UL44 in origin-dependent DNA replication in cells. J. Virol. 2008, 82:12574-12579.
    • (2008) J. Virol. , vol.82 , pp. 12574-12579
    • Sinigalia, E.1    Alvisi, G.2    Mercorelli, B.3    Coen, D.M.4    Pari, G.S.5    Jans, D.A.6    Ripalti, A.7    Palu, G.8    Loregian, A.9
  • 24
    • 33744950505 scopus 로고    scopus 로고
    • Human cytomegalovirus (HCMV) DNA polymerase processivity factor ppUL44 dimerizes in the cytosol before translocation to the nucleus
    • Alvisi G., Jans D.A., Ripalti A. Human cytomegalovirus (HCMV) DNA polymerase processivity factor ppUL44 dimerizes in the cytosol before translocation to the nucleus. Biochemistry 2006, 45:6866-6872.
    • (2006) Biochemistry , vol.45 , pp. 6866-6872
    • Alvisi, G.1    Jans, D.A.2    Ripalti, A.3
  • 25
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kappa B and I kappa B proteins: new discoveries and insights
    • Baldwin A.S. The NF-kappa B and I kappa B proteins: new discoveries and insights. Annu. Rev. Immunol. 1996, 14:649-683.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-683
    • Baldwin, A.S.1
  • 26
    • 0030935858 scopus 로고    scopus 로고
    • The tumor suppressor p53 is subject to both nuclear import and export, and both are fast, energy-dependent and lectin-inhibited
    • Middeler G., Zerf K., Jenovai S., Thulig A., Tschodrich-Rotter M., Kubitscheck U., Peters R. The tumor suppressor p53 is subject to both nuclear import and export, and both are fast, energy-dependent and lectin-inhibited. Oncogene 1997, 14:1407-1417.
    • (1997) Oncogene , vol.14 , pp. 1407-1417
    • Middeler, G.1    Zerf, K.2    Jenovai, S.3    Thulig, A.4    Tschodrich-Rotter, M.5    Kubitscheck, U.6    Peters, R.7
  • 27
    • 0034632056 scopus 로고    scopus 로고
    • Form of human p53 protein during nuclear transport in Xenopus laevis embryos
    • Hara T., Arai K., Koike K. Form of human p53 protein during nuclear transport in Xenopus laevis embryos. Exp. Cell Res. 2000, 258:152-161.
    • (2000) Exp. Cell Res. , vol.258 , pp. 152-161
    • Hara, T.1    Arai, K.2    Koike, K.3
  • 28
    • 33845427459 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: dual role of replication and transcription activator
    • Wang Y., Tang Q., Maul G.G., Yuan Y. Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: dual role of replication and transcription activator. J. Virol. 2006, 80:12171-12186.
    • (2006) J. Virol. , vol.80 , pp. 12171-12186
    • Wang, Y.1    Tang, Q.2    Maul, G.G.3    Yuan, Y.4
  • 29
    • 40149108605 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: involvement of host cellular factors
    • Wang Y., Li H., Tang Q., Maul G.G., Yuan Y. Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: involvement of host cellular factors. J. Virol. 2008, 82:2867-2882.
    • (2008) J. Virol. , vol.82 , pp. 2867-2882
    • Wang, Y.1    Li, H.2    Tang, Q.3    Maul, G.G.4    Yuan, Y.5
  • 30
    • 0030048573 scopus 로고    scopus 로고
    • Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures
    • Liptak L.M., Uprichard S.L., Knipe D.M. Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures. J. Virol. 1996, 70:1759-1767.
    • (1996) J. Virol. , vol.70 , pp. 1759-1767
    • Liptak, L.M.1    Uprichard, S.L.2    Knipe, D.M.3
  • 31
    • 0031743484 scopus 로고    scopus 로고
    • ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase
    • Burkham J., Coen D.M., Weller S.K. ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase. J. Virol. 1998, 72:10100-10107.
    • (1998) J. Virol. , vol.72 , pp. 10100-10107
    • Burkham, J.1    Coen, D.M.2    Weller, S.K.3
  • 32
    • 0037377759 scopus 로고    scopus 로고
    • Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins
    • Carrington-Lawrence S.D., Weller S.K. Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins. J. Virol. 2003, 77:4237-4247.
    • (2003) J. Virol. , vol.77 , pp. 4237-4247
    • Carrington-Lawrence, S.D.1    Weller, S.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.