Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16

Genes and Development

Volumn 13, Issue 13, 1999, Pages 1692-1703

  Liu, Yu ^a,d   Gong, Weimin ^a,b,e   Huang, C Chris ^a,c,f   Herr, Winship ^a   Cheng, Xiaodong ^a,b  

^a Cold Spring Harbor Laboratory ^*  (United States)

^b EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c STONY BROOK UNIVERSITY   (United States)

^d HONG KONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Hong Kong)

^e OHIO STATE UNIVERSITY   (United States)

^f MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

Crystal structure; DNA recognition; HSV; Protein VP16

Indexed keywords

AMINO ACID; CELL PROTEIN; DNA; REGULATOR PROTEIN; VIRUS PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DNA BINDING; HERPES SIMPLEX VIRUS; NONHUMAN; PRIORITY JOURNAL; VIRION;

DNA VIRUSES; HERPES; SIMPLEXVIRUS;

EID: 0033166256     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.13.13.1692     Document Type: Article

References (60)

1. Ace, C.I., M.A. Dalrymple, F.H. Ramsay, V.G. Preston, and C.M. Preston. 1988. Mutational analysis of the herpes simplex virus type 1 trans-inducing factor, Vmw65. J. Gen. Virol. 69: 2595-2605.
2. Brünger, A.T. 1992. X-PLOR. A system for X-ray crystallography and NMR, version 3.1, Yale University, New Haven, CT.
3. Campbell, M.E., J.W. Palfreman, and C.M. Preston. 1984. Identification of herpes simplex virus DNA sequences which encode a trans-acting polypeptide responsible for stimulation of immediate early transcription. J. Mol. Biol. 180: 1-19.
4. Carpenter, D.E. and V. Misra. 1992. Sequences of the bovine herpesvirus 1 homologue of herpes simplex virus α-trans-inducing factor (UL48). Gene 119: 259-263.
5. Carson, M. 1991. Ribbons 2.0. J. Appl. Crystallogr. 24: 958-961.
6. Cleary, M.A., P.S. Pendergrast, and W. Herr. 1997. Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking. Proc. Natl. Acad. Sci. 94: 8450-8455.
7. Cousens, D.J., R. Greaves, C.R. Coding, and P. O'Hare. 1989. The C-terminal 79 amino acids of the herpes simplex virus regulatory protein, Vmw65, efficiently activate transcription in yeast and mammalian cells in chimeric DNA-binding proteins. EMBO J. 8: 2337-2342.
8. Dalrymple, M.A., D.J. McGeoch, A.J. Davison, and C.M. Preston. 1985. DNA sequence of the herpes simplex virus type 1 gene whose product is responsible for transcriptional activation of immediate early promoters. Nucleic Acids Res. 13: 7865-7879.
9. Davison, A.J. and J.E. Scott. 1986. The complete DNA sequence of varicella-zoster virus. J. Gen. Virol. 67: 1759-1816.
10. Donaldson, L. and J.P. Capone. 1992. Purification and characterization of the carboxyl-terminal transactivation domain of Vmw65 from herpes simplex virus type I. J. Biol. Chem. 267: 1411-1414.
11. 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.
12. Furey, W. and S. Swaminathan. 1997. PHASES-95: A program package for the processing and analysis of diffraction data from macromolecules. Methods Enzymol. 277: 590-620.
13. Goto, H., S. Motomura, A.C. Wilson, R.N. Freiman, Y. Nakabeppu, K. Fukushima, M. Fujishima, W. Herr, and T. Nishimoto. 1997. A single-point mutation in HCF causes temperature-sensitive cell-cycle arrest and disrupts VP16 function. Genes & Dev. 11: 726-737.
14. 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 proteins and target TAATGARAT sequences. J. Virol. 64: 2716-2724.
15. Haigh, A., R.F. Greaves, and P. O'Hare. 1990. Interference with the assembly of a virus-host transcription complex by peptide competition. Nature 344: 257-259.
16. 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.
17. Hendrickson, W.A., J.R. Horton, and D.M. LeMaster. 1990. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. EMBO J. 9: 1665-1672.
18. Herr, W. and M.A. Cleary. 1995. The POU domain: Versatility in transcriptional regulation by a flexible two-in-one DNA binding domain. Genes & Dev. 9: 1679-1693.
19. Huang, C.C. and W. Herr. 1996. Differential control of transcription by homologous homeodomain coregulators. Mol. Cell. Biol. 16: 2967-2976.
20. Jancarik, J. and S.H. Kim. 1991. Sparse matrix sampling: A screening method for crystallization of proteins. J. Appl. Crystallogr. 24: 409-411.
21. Jones, T.A., J.Y. Zou, S.W. Cowan, and M. Kjeldgard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. A47: 110-119.
22. Klemm, J.D., M.A. Rould, R. Aurora, W. Herr, and C.O. Pabo. 1994. Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell 77: 21-32.
23. Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
24. Kristie, T.M., J.H. LeBowowitz, and P.A. Sharp. 1989. The octamer-binding proteins form multi-protein-DNA complexes with the HSV α-TIF regulatory protein. EMBO J. 8: 4229-4238.
25. Kristie, T.M. and P.A. Sharp. 1990. Interactions of the Oct-1 POU subdomains with specific DNA sequences and the HSV α-trans-activator protein. Genes & Dev. 4: 2383-2396.
26. Kristie, T.M., J.L. Pomerantz, T.C. Twomey, S.A. Parent, and P.A. Sharp. 1995. The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides. J. Biol. Chem. 270: 4387-4394.
27. LaBoissière, 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.
28. 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.
29. Lai, J.-S., M.A. Cleary, and W. Herr. 1992. A single amino acid exchange transfers VP16-induced positive control from the Oct-1 to the Oct-2 homeo domain. Genes & Dev. 6: 2058-2065.
30. Laskowski, R.A., M.W. MacArthur, D.S. Moss, and J.M. Thornton. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
31. Li, T., M.R. Stark, A.D. Johnson, and C. Wolberger. 1995. Crystal structure of the MATa1/α2 homeodomain heterodimer bound to DNA. Science 270: 262-269.
32. 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.
33. Misra, V., S. Walker, P. Yang, S. Hayes, and P. O'Hare. 1996. Conformational alteration of Oct-1 upon DNA binding dictates selectivity in differential interactions with related transcriptional coactivator. Mol. Cell. Biol. 16: 4404-4413.
34. Nicholls, A., K.A. Sharp, and B. Honig. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Protein Struct. Funct. Genet. 11: 281-296.
35. O'Hare, P. 1993. The virion transactivator of herpes simplex virus. Semin. Virol. 4: 145-155.
36. 1H NMR. Biochemistry 31: 4150-4156.
37. Otwinowski, Z. and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
38. Pearson, W.R. and D.J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. 85: 2444-2448.
39. 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.
40. Ramakrishnan, V. and V. Biou. 1997. Treatment of MAD data as a specific case of MIR. Methods Enzymol. 276: 538-557.
41. Sadowski, I., J. Ma, S.J. Triezenberg, and M. Ptashne. 1988. GAL4-VP16: An unusual potent transcriptional activator. Nature 335: 551-557.
42. Shaw, P., J. Knez, and J.P. Capone. 1995. Amino acid substitutions in the herpes simplex virus transactivator VP16 uncouple direct protein-protein interaction and DNA binding from complex assembly and transactivation. J. Biol. Chem. 270: 29030-29037.
43. Shen, F., S.J. Triezenberg, P. Hensley, D. Porter, and J.R. Knutson. 1996. Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. J. Biol. Chem. 271: 4827-4837.
44. 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 virus type 1 VP16-induced complex: VP16 peptide inhibition and mutational analysis of host cell factor requirements. J. Virol. 71: 3886-3894.
45. Smibert, C.A., B. Popova, P. Xiao, J.A. Capone, and J.R. Smiley. 1994. Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs. J. Virol. 68: 2339-2346.
46. Smith, D.O. and K.S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene 67: 31-40.
47. Stern, S., M. Tanaka, and W. Herr. 1989. The Oct-1 homeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16. Nature 341: 624-630.
48. 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.
49. Telford, E.A., M.S. Watson, K. McBride, and A.J. Davison. 1992. The DNA sequence of equine herpesvirus-1. Virology 189: 304-316.
50. Thompson, C.C. and S.L. McKnight. 1992. Anatomy of an enhancer. Trends Genet. 8: 232-236.
51. Triezenberg, S.J., R.G. Kingsbury, and S.L. McKnight. 1988. Functional dissection of VP16, the trans-activator of herpes simplex virus immediate early gene expression. Genes & Dev. 2: 718-729.
52. Uesugi, M., O. Nyanguile, H. Lu, A.J. Levine, and G.L. Verdine. 1997. Induced a helix in the VP16 activation domain upon binding to a human TAF. Science 277: 1310-1313.
53. 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.
54. Wang, B.-C. 1985. Resolution of phase ambiguity in macromolecular crystallography. Methods Enzymol. 115: 90-112.
55. Werstuck, G. and J.P. Capone. 1989. Mutational analysis of the herpes simplex virus trans-inducing factor Vmw65. Gene 75: 213-224.
56. 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.
57. 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.
58. Wu, T.-J., G. Monokian, D. Mark, and C.R. Wobbe. 1994. Transcriptional activation by herpes simplex virus type 1 VP16 in vitro and its inhibition by oligopeptide. Mol. Cell. Biol. 14: 3484-3493.
59. Xu, R.-M., C. Koch, Y. Liu, J.R. Horton, D. Knapp, K. Nasmyth, and X. Cheng. 1997. Crystal structure of the DNA-binding domain of Mbpl, a transcription factor important in cell-cycle control of DNA synthesis. Structure 5: 349-358.
60. Yanagida, N., S. Yoshida, K. Nazerian, and L.F. Lee. 1993. Nucleotide and predicted amino acid sequence of Marek's disease virus homologues of herpes simplex virus major tegument proteins. J. Gen. Virol. 74: 1837-1845.