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Volumn 20, Issue 3, 2000, Pages 919-928

Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR PROTEIN; TRANSCRIPTION FACTOR;

EID: 0033959126     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.3.919-928.2000     Document Type: Article
Times cited : (26)

References (50)
  • 1
    • 0026518157 scopus 로고
    • A Drosophila CREB/ATF transcriptional activator binds to both fat body- and liver-specific regulatory elements
    • Abel, T., R. Bhatt, and T. Maniatis. 1992. A Drosophila CREB/ATF transcriptional activator binds to both fat body- and liver-specific regulatory elements. Genes Dev. 6:466-480.
    • (1992) Genes Dev. , vol.6 , pp. 466-480
    • Abel, T.1    Bhatt, R.2    Maniatis, T.3
  • 2
    • 0028231273 scopus 로고
    • Drosophila kelch motif is derived from a common enzyme fold
    • Bork, P., and R. F. Doolittle. 1994. Drosophila kelch motif is derived from a common enzyme fold. J. Mol. Biol. 234:1277-1282.
    • (1994) J. Mol. Biol. , vol.234 , pp. 1277-1282
    • Bork, P.1    Doolittle, R.F.2
  • 3
    • 0030034644 scopus 로고    scopus 로고
    • The G-protein nanomachine
    • Clapham, D. E. 1996. The G-protein nanomachine. Nature 379:297-299.
    • (1996) Nature , vol.379 , pp. 297-299
    • Clapham, D.E.1
  • 4
    • 0027336003 scopus 로고
    • The dTAFIISO subunit of Drosophila TFIID contains beta-transducin repeats
    • Dynlacht, B. D., R. O. Weinzierl, A. Admon, and R. Tjian. 1993. The dTAFIISO subunit of Drosophila TFIID contains beta-transducin repeats. Nature 363:176-179.
    • (1993) Nature , vol.363 , pp. 176-179
    • Dynlacht, B.D.1    Weinzierl, R.O.2    Admon, A.3    Tjian, R.4
  • 5
    • 0030687635 scopus 로고    scopus 로고
    • Viral mimicry: Common mode of association with HCF by VP16 and the cellular protein LZIP
    • Freiman, R. N., and W. Herr. 1997. Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP. Genes Dev. 11:3122-3127.
    • (1997) Genes Dev. , vol.11 , pp. 3122-3127
    • Freiman, R.N.1    Herr, W.2
  • 6
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin
    • Gaudet, R., A. Bohm, and P. B. Sigler. 1996. Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin. Cell 87:577-588.
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 7
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman, O. B., Jr., J. G. Krupnick, V. V. Gurevich, J. L. Benovic, and J. H. Keen. 1997. Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. J. Biol. Chem. 272:15017-15022.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15017-15022
    • Goodman O.B., Jr.1    Krupnick, J.G.2    Gurevich, V.V.3    Benovic, J.L.4    Keen, J.H.5
  • 9
    • 0025375785 scopus 로고
    • Structural requirements in the herpes simplex virus type 1 transactivator Vmw65 for interaction with the cellular octamer-binding protein and target TAATGARAT sequences
    • Greaves, R. F., and P. O'Hare. 1990. Structural requirements in the herpes simplex virus type 1 transactivator Vmw65 for interaction with the cellular octamer-binding protein and target TAATGARAT sequences. J. Virol. 64: 2716-2724.
    • (1990) J. Virol. , vol.64 , pp. 2716-2724
    • Greaves, R.F.1    O'Hare, P.2
  • 10
    • 0025194256 scopus 로고
    • Interference with the assembly of a virus-host transcription complex by peptide competition
    • Haigh, A., R. Greaves, and P. O'Hare. 1990. Interference with the assembly of a virus-host transcription complex by peptide competition. Nature 344: 257-259.
    • (1990) Nature , vol.344 , pp. 257-259
    • Haigh, A.1    Greaves, R.2    O'Hare, P.3
  • 11
    • 0027472266 scopus 로고
    • Mapping of a major surface-exposed site in herpes simplex virus protein Vmw65 to a region of direct interaction in a transcription complex assembly
    • Hayes, S., and P. O'Hare. 1993. Mapping of a major surface-exposed site in herpes simplex virus protein Vmw65 to a region of direct interaction in a transcription complex assembly. J. Virol. 67:852-862.
    • (1993) J. Virol. , vol.67 , pp. 852-862
    • Hayes, S.1    O'Hare, P.2
  • 12
    • 9344250068 scopus 로고    scopus 로고
    • Differential control of transcription by homologous homeodomain coregulator
    • Huang, C. C., and W. Herr. 1996. Differential control of transcription by homologous homeodomain coregulator. Mol. Cell. Biol. 16:2967-2976.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2967-2976
    • Huang, C.C.1    Herr, W.2
  • 13
    • 0040294788 scopus 로고    scopus 로고
    • Analysis of functional domains of the host cell factor involved in VP16 complex formation
    • Hughes, T. A., S. La Boissiere, and P. O'Hare. 1999. Analysis of functional domains of the host cell factor involved in VP16 complex formation. J. Biol. Chem. 274:16437-16443.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16437-16443
    • Hughes, T.A.1    La Boissiere, S.2    O'Hare, P.3
  • 14
    • 0032897973 scopus 로고    scopus 로고
    • Herpes simplex virus transactivator VP16 discriminates between HCF-1 and a novel family member, HCF-2
    • Johnson, K. M., S. S. Mahajan, and A. C. Wilson. 1999. Herpes simplex virus transactivator VP16 discriminates between HCF-1 and a novel family member, HCF-2. J. Virol. 73:3930-3940.
    • (1999) J. Virol. , vol.73 , pp. 3930-3940
    • Johnson, K.M.1    Mahajan, S.S.2    Wilson, A.C.3
  • 15
    • 0032080221 scopus 로고    scopus 로고
    • Ciao 1 is a novel WD40 protein that interacts with the tumor suppressor protein WT1
    • Johnstone, R. W., J. Wang, N. Tommerup, H. Vissing, T. Roberts, and Y. Shi. 1998. Ciao 1 is a novel WD40 protein that interacts with the tumor suppressor protein WT1. J. Biol. Chem. 273:10880-10887.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10880-10887
    • Johnstone, R.W.1    Wang, J.2    Tommerup, N.3    Vissing, H.4    Roberts, T.5    Shi, Y.6
  • 16
    • 0029031542 scopus 로고
    • Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation
    • Klemm, R. D., J. A. Goodrich, S. Zhou, and R. Tjian. 1995. Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. Proc. Natl. Acad. Sci. USA 92:5788-5792.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5788-5792
    • Klemm, R.D.1    Goodrich, J.A.2    Zhou, S.3    Tjian, R.4
  • 17
    • 0030825790 scopus 로고    scopus 로고
    • Residues in the WD repeats of Tup1 required for interaction with α2
    • Komachi, K., and A. D. Johnson. 1997. Residues in the WD repeats of Tup1 required for interaction with α2. Mol. Cell. Biol. 17:6023-6028.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6023-6028
    • Komachi, K.1    Johnson, A.D.2
  • 18
    • 0024815587 scopus 로고
    • The octamer-binding proteins form multi-protein-DNA complexes with the HSV αTIF regulatory protein
    • Kristie, T. M., J. H. LeBowitz, and P. A. Sharp. 1989. The octamer-binding proteins form multi-protein-DNA complexes with the HSV αTIF regulatory protein. EMBO J. 8:4229-4238.
    • (1989) EMBO J. , vol.8 , pp. 4229-4238
    • Kristie, T.M.1    LeBowitz, J.H.2    Sharp, P.A.3
  • 19
    • 0028904801 scopus 로고
    • The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides
    • Kristie, T. M., J. L. Pomerantz, T. C. Twomey, S. A. Parent, and P. A. Sharp, A. 1995. The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides. J. Biol. Chem. 270:4387-4394.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4387-4394
    • Kristie, T.M.1    Pomerantz, J.L.2    Twomey, T.C.3    Parent, S.A.4    Sharp, P.A.5    A6
  • 20
    • 0030967614 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus
    • Krupnick, J. G., O. B. Goodman, Jr., J. H. Keen, and J. L. Benovic. 1997. Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus. J. Biol. Chem. 272:15011-15016.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15011-15016
    • Krupnick, J.G.1    Goodman O.B., Jr.2    Keen, J.H.3    Benovic, J.L.4
  • 21
    • 0040036654 scopus 로고    scopus 로고
    • HCF-dependent nuclear import of VP16
    • La Boissiere, S., T. Hughes, and P. O'Hare. 1999. HCF-dependent nuclear import of VP16. EMBO J. 18:480-489.
    • (1999) EMBO J. , vol.18 , pp. 480-489
    • La Boissiere, S.1    Hughes, T.2    O'Hare, P.3
  • 22
    • 0030667738 scopus 로고    scopus 로고
    • Concerted activity of host cell factor subregions in promoting stable VP16 complex assembly and preventing interference by the acidic activation domain
    • LaBoissiere, S., S. Walker, and P. O'Hare. 1997. Concerted activity of host cell factor subregions in promoting stable VP16 complex assembly and preventing interference by the acidic activation domain. Mol. Cell. Biol. 17: 7108-7118.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7108-7118
    • LaBoissiere, S.1    Walker, S.2    O'Hare, P.3
  • 23
    • 0026452291 scopus 로고
    • A single amino acid exchange transfers VP16-induced positive control from Oct-1 to the Oct-2 homeo domain
    • Lai, J.-S., M. A. Cleary, and W. Herr. 1992. A single amino acid exchange transfers VP16-induced positive control from Oct-1 to the Oct-2 homeo domain. Genes Dev. 6:2058-2065.
    • (1992) Genes Dev. , vol.6 , pp. 2058-2065
    • Lai, J.-S.1    Cleary, M.A.2    Herr, W.3
  • 24
    • 0030989157 scopus 로고    scopus 로고
    • Interdigitated residues within a small region of VP16 interact with Oct-1, HCF, and DNA
    • Lai, J.-S., and W. Herr. 1997. Interdigitated residues within a small region of VP16 interact with Oct-1, HCF, and DNA. Mol. Cell. Biol. 17:3937-3946.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3937-3946
    • Lai, J.-S.1    Herr, W.2
  • 25
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MATα2 homeodomain heterodimer hound to DNA
    • Li, T., M. R. Stark, A. D. Johnson, and C. Wolberger. 1995. Crystal structure of the MATa1/MATα2 homeodomain heterodimer hound to DNA. Science 270:262-269.
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 26
    • 0033166256 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16
    • Liu, Y., W. Gong, C. C. Huang, W. Herr, and X. Cheng. 1999. Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16. Genes Dev. 13:1692-1703.
    • (1999) Genes Dev. , vol.13 , pp. 1692-1703
    • Liu, Y.1    Gong, W.2    Huang, C.C.3    Herr, W.4    Cheng, X.5
  • 27
    • 0032961174 scopus 로고    scopus 로고
    • Selected elements of herpes simplex virus accessory factor HCF are highly conserved in Caenorhabditis elegans
    • Liu, Y., M. O. Hengartner, and W. Herr. 1999. Selected elements of herpes simplex virus accessory factor HCF are highly conserved in Caenorhabditis elegans. Mol. Cell. Biol. 19:909-915.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 909-915
    • Liu, Y.1    Hengartner, M.O.2    Herr, W.3
  • 28
    • 0030850014 scopus 로고    scopus 로고
    • Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cell factor
    • Lu, R., P. Yang, P. O'Hare, and V. Misra. 1997. Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cell factor. Mol. Cell. Biol. 17:5117-5126.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5117-5126
    • Lu, R.1    Yang, P.2    O'Hare, P.3    Misra, V.4
  • 29
    • 0031878579 scopus 로고    scopus 로고
    • The herpesvirus transactivator VP16 mimics a human basic domain leucine zipper protein, Luman, in its interaction with HCF
    • Lu, R., P. Yang, S. Padmakumar, and V. Misra. 1998. The herpesvirus transactivator VP16 mimics a human basic domain leucine zipper protein, Luman, in its interaction with HCF. J. Virol. 72:6291-6297.
    • (1998) J. Virol. , vol.72 , pp. 6291-6297
    • Lu, R.1    Yang, P.2    Padmakumar, S.3    Misra, V.4
  • 31
    • 0001682893 scopus 로고
    • The virion transactivator of herpes simplex virus
    • O'Hare, P. 1993. The virion transactivator of herpes simplex virus. Semin. Virol. 4:145-155.
    • (1993) Semin. Virol. , vol.4 , pp. 145-155
    • O'Hare, P.1
  • 32
    • 0026468492 scopus 로고
    • Recognition of the surface of a homeo domain protein
    • Pomerantz, J. L., T. M. Kristie, and P. A. Sharp. 1992. Recognition of the surface of a homeo domain protein. Genes Dev. 6:2047-2057.
    • (1992) Genes Dev. , vol.6 , pp. 2047-2057
    • Pomerantz, J.L.1    Kristie, T.M.2    Sharp, P.A.3
  • 33
    • 0032485075 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller
    • Renault, L., N. Nassar, I. Vetter, J. Becker, C. Klebe, M. Roth, and A. Wittinghofer. 1998. The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Nature 392: 97-101.
    • (1998) Nature , vol.392 , pp. 97-101
    • Renault, L.1    Nassar, N.2    Vetter, I.3    Becker, J.4    Klebe, C.5    Roth, M.6    Wittinghofer, A.7
  • 34
    • 0030951418 scopus 로고    scopus 로고
    • Protein interactions in the herpes simplex type 1 VP16 induced complex: VP16 peptide inhibition and mutational analysis of the host cell factor requirements
    • Simmen, K. A., A. Newell, M. Robinson, J. S. Mills, G. Canning, R. Handa, K. Parkes, N. Borkakoti, and R. Jupp. 1997. Protein interactions in the herpes simplex type 1 VP16 induced complex: VP16 peptide inhibition and mutational analysis of the host cell factor requirements. J. Virol. 71:3886-3894.
    • (1997) J. Virol. , vol.71 , pp. 3886-3894
    • Simmen, K.A.1    Newell, A.2    Robinson, M.3    Mills, J.S.4    Canning, G.5    Handa, R.6    Parkes, K.7    Borkakoti, N.8    Jupp, R.9
  • 35
    • 0026699358 scopus 로고
    • A cyclic AMP-responsive element-binding transcriptional activator in Drosophila melanogaster, dCREB-A, is a member of the leucine zipper family
    • Smolik, S. M., R. E. Rose, and R. H. Goodman. 1992. A cyclic AMP-responsive element-binding transcriptional activator in Drosophila melanogaster, dCREB-A, is a member of the leucine zipper family. Mol. Cell. Biol. 12:4123-4131.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4123-4131
    • Smolik, S.M.1    Rose, R.E.2    Goodman, R.H.3
  • 36
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a GA protein βγ dimer at 2.1 Å resolution
    • Sondek, J., A. Bohm, D. G. Lambright, H. E. Hamm, and P. B. Sigler. 1996. Crystal structure of a GA protein βγ dimer at 2.1 Å resolution. Nature 379:369-374.
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 37
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal ligand-binding region of integrin α subunits into a β-propeller domain
    • Springer, T. A. 1997. Folding of the N-terminal ligand-binding region of integrin α subunits into a β-propeller domain. Proc. Natl. Acad. Sci. USA 94:65-72.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 38
    • 0026296834 scopus 로고
    • The herpes simplex virus trans-activator VP16 recognizes the Oct-1 homeo domain: Evidence for a homeo domain recognition subdomain
    • Stern, S., and W. Herr. 1991. The herpes simplex virus trans-activator VP16 recognizes the Oct-1 homeo domain: evidence for a homeo domain recognition subdomain. Genes Dev. 5:2555-2566.
    • (1991) Genes Dev. , vol.5 , pp. 2555-2566
    • Stern, S.1    Herr, W.2
  • 39
    • 0024465662 scopus 로고
    • The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16
    • Stern, S., M. Tanaka, and W. Herr. 1989. The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16. Nature 341:624-630.
    • (1989) Nature , vol.341 , pp. 624-630
    • Stern, S.1    Tanaka, M.2    Herr, W.3
  • 40
    • 0032514995 scopus 로고    scopus 로고
    • Atomic structure of clathrin: A beta propeller terminal domain joins an alpha zigzag linker
    • ter Haar, E., A. Musacchio, S. C. Harrison, and T. Kirchhausen. 1998. Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker. Cell 95:563-573.
    • (1998) Cell , vol.95 , pp. 563-573
    • Ter Haar, E.1    Musacchio, A.2    Harrison, S.C.3    Kirchhausen, T.4
  • 43
    • 0027169855 scopus 로고
    • Transcriptional activation by the acidic domain of Vmw65 requires the intergrity of the domain and additional determinants distinct from those necessary for TFIIB binding
    • Walker, S., R. Greaves, and P. O'Hare. 1993. Transcriptional activation by the acidic domain of Vmw65 requires the intergrity of the domain and additional determinants distinct from those necessary for TFIIB binding. Mol. Cell. Biol. 13:5233-5244.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5233-5244
    • Walker, S.1    Greaves, R.2    O'Hare, P.3
  • 44
    • 0027983889 scopus 로고
    • Site-specific conformational alteration of the Oct-1 POU domain-DNA complex as the basis for differential recognition by Vmw65 (VP16)
    • Walker, S., S. Hayes, and P. O'Hare. 1994. Site-specific conformational alteration of the Oct-1 POU domain-DNA complex as the basis for differential recognition by Vmw65 (VP16). Cell 79:841-852.
    • (1994) Cell , vol.79 , pp. 841-852
    • Walker, S.1    Hayes, S.2    O'Hare, P.3
  • 47
    • 0030863636 scopus 로고    scopus 로고
    • VP16 targets an amino-terminal domain of HCF involved in cell-cycle progression
    • Wilson, A. C., R. N. Freiman, H. Goto, T. Nishimoto, and W. Herr. 1997. VP16 targets an amino-terminal domain of HCF involved in cell-cycle progression. Mol. Cell. Biol. 17:6139-6146.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6139-6146
    • Wilson, A.C.1    Freiman, R.N.2    Goto, H.3    Nishimoto, T.4    Herr, W.5
  • 48
    • 0027328280 scopus 로고
    • The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein
    • Wilson, A. C., K. LaMarco, M. G. Peterson, and W. Herr. 1993. The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein. Cell 74:115-125.
    • (1993) Cell , vol.74 , pp. 115-125
    • Wilson, A.C.1    LaMarco, K.2    Peterson, M.G.3    Herr, W.4
  • 49
    • 0028860944 scopus 로고
    • The HCF repeat is an unusual proteolytic cleavage signal
    • Wilson, A. C., M. G. Peterson, and W. Herr. 1995. The HCF repeat is an unusual proteolytic cleavage signal. Genes Dev. 9:2445-2458.
    • (1995) Genes Dev. , vol.9 , pp. 2445-2458
    • Wilson, A.C.1    Peterson, M.G.2    Herr, W.3
  • 50
    • 0028218432 scopus 로고
    • Transcriptional activation by herpes simplex virus type 1 VP16 in vitro and its inhibition by oligopeptides
    • Wu, T. J., G. Monokian, D. F. Mark, and C. R. Wobbe. 1994. Transcriptional activation by herpes simplex virus type 1 VP16 in vitro and its inhibition by oligopeptides. Mol. Cell. Biol. 14:3484-3493.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3484-3493
    • Wu, T.J.1    Monokian, G.2    Mark, D.F.3    Wobbe, C.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.