The herpes simplex virus VP16-induced complex: Mechanisms of combinatorial transcriptional regulation

Cold Spring Harbor Symposia on Quantitative Biology

Volumn 63, Issue , 1998, Pages 599-607

  Herr, W ^a  

^a Watson School of Biological Sciences   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TRANSCRIPTION FACTOR; VIRUS PROTEIN; DNA BINDING PROTEIN; OCTAMER TRANSCRIPTION FACTOR 1; OCTAMER TRANSCRIPTION FACTOR 2; PROTEIN VP16; VIRAL PROTEIN;

B LYMPHOCYTE; BINDING SITE; COMPLEX FORMATION; CONFERENCE PAPER; DNA SEQUENCE; HERPES SIMPLEX VIRUS; NONHUMAN; NUCLEAR LOCALIZATION SIGNAL; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; TRANSCRIPTION REGULATION; VIRION; CELL ACTIVATION; CELL PROLIFERATION; COMBINATORIAL CHEMISTRY; DNA RESPONSIVE ELEMENT; ENZYME SPECIFICITY; GENETIC ASSOCIATION; GENETIC CODE; GENETIC TRANSCRIPTION; PROTEIN BINDING; PROTEIN DNA BINDING; PROTEIN INTERACTION; REGULATORY SEQUENCE; VIRAL GENETICS;

EID: 0032466794     PISSN: 00917451     EISSN: None     Source Type: Book Series    
DOI: 10.1101/sqb.1998.63.599     Document Type: Conference Paper

References (61)

1. apRhys C.M.J., Ciufo D.M., O'Neill E.A., Kelly T.J., and Hayward G.S. 1989. Overlapping octamer and TAATGARAT motifs in the VF65-response elements in herpes simplex virus immediate-early promoters represent independent binding sites for cellular nuclear factor III. J. Virol. 63: 2798.
2. Assa-Munt N., Mortishire-Smith R.J., Aurora R., Herr W., and Wright P.E. 1993. The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage λ repressor DNA-binding domain. Cell 73: 193.
3. Babb, R., Cleary M.A., and Herr W. 1997. OCA-B is a functional analog of VP16 but targets a separate surface of the Oct-1 POU domain. Mol. Cell. Biol. 17: 7295.
4. Baumruker T., Sturm R., and Herr W. 1988. OBP100 binds remarkably degenerate octamer motifs through specific interactions with flanking sequences. Genes Dev. 2: 1400.
5. Bohmann D., Keller W., Dale T., Scholer H.R., Tebb G., and Mattaj I.W. 1987. A transcription factor which binds to the enhancers of SV40, immunoglobulin heavy chain and U2 snRNA genes. Nature 325: 268.
6. Bork P. and Doolittle R.F. 1994. Drosophila kelch motif is derived from a common enzyme fold. J. Mol. Biol. 236: 1277.
7. Cleary M.A. and Herr W. 1995. Mechanisms for flexibility in DNA sequence recognition and VP16-induced complex formation by the Oct-1 POU domain. Mol. Cell. Biol. 15: 2090.
8. Cleary M.A., Pendergrast P.S., and Herr W. 1997. Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking. Proc. Natl. Acad. Sci. 9-4: 8450.
9. Cleary M.A., Stem S., Tanaka M., and Herr W. 1993. Differential positive control by Oct-1 and Oct-2: Activation of a transcriptionally silent motif through Oct-1 and VP16 corecruitment. Genes Dev. 7: 72.
10. Cousens D.J., Greaves R., Coding C.R., and O'Hare P. 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.
11. Das G., Hinkley C.S., and Herr W. 1995. Basal promoter elements as a selective determinant of transcriptional activator function. Nature 374: 657.
12. Dekker N., Cox M., Boelens R., Verrijzer C., van der Vliet P.C., and Kaptein R. 1993. Solution structure of the POU-specific DNA-binding domain of Oct-1. Nature 362: 852.
13. C largest subunit that bears sequence similarities to the Oct-1 coactivator OBF-1. Genes Dev. 12: 3528.
14. Freiman R.N. and Herr W. 1997. Viral mimicry: Common mode of association with HCF by VP16 and the cellular protein LZAIP. Genes Dev. 11: 3122.
15. Gerster T. and Roeder R.G. 1988. A herpesvirus trans-activating protein interacts with transcription factor OTF-1 and other cellular proteins. Proc. Natl. Acad. Sci. 85: 6347.
16. Goto H., Motomura S., Wilson A.C., Freiman R.N., Nakabeppu Y., Fukushima K., Fujishima M., Herr W., and Nishimoto T. 1997. A single-point mutation in HCF causes temperature-sensitive cell-cycle arrest and disrupts VP16 function. Genes Dev. 11: 726.
17. Greaves R.F. and O'Hare P. 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.
18. Gstaiger M., Knoepfel L., Georgiev O., Schaffner W., and Hovens C.M. 1995. A B-cell coactivator of octamer-binding transcription factors. Nature 373: 360.
19. Hayes S. and O'Hare P. 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.
20. Herr W. and Cleary M.A. 1995. The POU domain: Versatility in transcriptional regulation by a flexible two-in-one DNA binding domain. Genes Dev. 9: 1679.
21. Herr W., Sturm R.A., Clerc R.G., Corcoran L.M., Baltimore D., Sharp P.A., Ingraham H.A., Rosenfeld M.G., Finney M., Ruvkun G., and Horvitz H.R. 1988. The POU domain: A large conserved region in the mammalian pit-1, oct-1, oct-2, and Caenorhabditis elegans unc-86 gene products. Genes Dev. 2: 1513.
22. Huang C.C. and Herr W. 1996. Differential control of transcription by homologous homeodomain coregulators. Mol. Cell. Biol. 16: 2967.
23. Katan M., Haigh A., Verrijzer C.P., van der Vliet P.C., and O'Hare P. 1990. Characterization of a cellular factor which interacts functionally with Oct-1 in the assembly of a multicomponent transcription complex. Nucleic Acids Res. 18: 6871.
24. Klemm J.D., Rould M.A., Aurora R., Herr W., and Pabo C.O. 1994. Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell 77: 21.
25. Kristie T.M. 1997. The mouse homologue of the human transcription factor C1 (host cell factor). J. Biol. Chem. 272: 26749.
26. Kristie T.M. and Sharp P.A. 1990. Interactions of the Oct-1 POU subdomains with specific DNA sequences and the HSV α-trans-activator protein. Genes Dev. 4: 2383.
27. Kristie T.M., LeBowitz J.H., and Sharp P.A. 1989. The octamer-binding proteins form multi-protein-DNA complexes with the HSV α-TIF regulatory protein. EMBO J. 8: 4229.
28. Kristie T.M., Pomerantz J.L., Twomey T.C., Parent S.A., and Sharp P.A. 1995. The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides. J. Biol. Chem. 270: 4387.
29. LaBoissiére S., Walker S., and O'Hare P. 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.
30. Lai J.-S. and Herr W. 1997. Interdigitated residues within a small region of VP16 interact with Oct-1, HCF, and DNA. Mol. Cell. Biol. 17: 3937.
31. Lai J.-S., Cleary M.A., and Herr W. 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.
32. Li T., Stark M.R., Johnson A.D., and Wolberger C. 1995. Crystal structure of the MATa1/α2 homeodomain heterodimer bound to DNA. Science 270: 262.
33. Liu Y., Hengartner M.O., and Herr W. 1999. Selected elements of herpes simplex virus accessory factor HCF are highly conserved in Caenorhabditis elegans. Mol. Cell. Biol. 19: 909.
34. Lu R., Yang P., O'Hare P., and Misra V. 1997. Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cellular factor. Mol. Cell. Biol. 17: 5117.
35. Lu R., Yang P., Padmakumar S., and Misra V. 1998. The herpesvirus transactivator VP16 mimics a human basic domain leucine zipper protein, Luman, in its interaction with HCF. Mol. Cell. Biol. 72: 6291.
36. Luo Y. and Roeder R.G. 1995. Cloning, functional characterization and mechanism of action of the B cell-specific transcriptional coactivator OCA-B. Mol. Cell. Biol. 15: 4115.
37. Luo Y., Fujii H., Gerster T., and Roeder R.G. 1992. A novel B cell-derived coactivator potentiates the activation of immunoglobulin promoters by octamer-binding transcription factors. Cell 71: 231.
38. Misra V., Walker S., Yang P., Hayes S., and O'Hare P. 1996. Conformational alteration of Oct-1 upon DNA binding dictates selectivity in differential interactions with related transcriptional coactivator. Mol. Cell. Biol. 16: 4404.
39. C. Mol. Cell. Biol. 16: 1955.
40. Pomerantz J.L., Kristie T.M., and Sharp P.A. 1992. Recognition of the surface of a homeo domain protein. Genes Dev. 6: 2047.
41. R3: Structural differences between consensus and non-consensus half-sites. Structure 1: 227.
42. Roizman B. and Sears A.E. 1990. Herpes simplex viruses and their replication. In Virology, 2nd edition (ed. B.N. Fields et al.), p. 1795. Raven Press, New York.
43. Sadowski I., Ma J., Triezenberg S.J., and Ptashne M. 1988. GAL4-VP16: An unusual potent transcriptional activator. Nature 335: 551.
44. Singh H., Sen R., Baltimore D., and Sharp P.A. 1986. A nuclear factor that binds to a conserved sequence motif in transcriptional control elements of immunoglobulin genes. Nature 319: 154.
45. Sivaraja M., Botfield M.C., Mueller M., Jancso A., and Weiss M.A. 1994. Solution structure of a POU-specific homeodomain: 3D-NMR studies of human B-cell transcription factor Oct-2. Biochemistry 33: 9845.
46. Sive H.L. and Roeder R.G. 1986. Interaction of a common factor with conserved promoter and enhancer rsequences in histone H2B, immunoglobulin, and U2 small nuclear RNA (snRNA) genes. Proc. Natl. Acad. Sci. 83: 6382.
47. Staudt L.M., Singh H., Sen R., Wirth T., Sharp P.A., and Baltimore D. 1986. A lymphoid-specific protein binding to the octamer motif of immunoglobulin genes. Nature 323: 640.
48. Stern S. and Herr W. 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.
49. Stern S., Tanaka M., and Herr W. 1989. The Oct-1 homeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16. Nature 341: 624.
50. Strubin M., Newell J.W., and Matthias P. 1995. OBF-1, a novel B cell-specific coactivator that stimulates immunoglobulin promoter activity through association with octamer-binding proteins. Cell 80: 497.
51. Sturm R.A. and Herr W. 1988. The POU domain is a bipartite DNA-binding structure. Nature 336: 601.
52. Tanaka M. and Herr W. 1990. Differential transcriptional activation by Oct-1 andf Oct-2: Interdependent activation domains induce Oct-2 phosphorylation. Cell 60: 375.
53. Tanaka M., Grossniklaus U., Herr W., and Hernandez N. 1988. Actcivation of the U2 snRNA promoter by the octamer motif defines a new class of RNA polymerase II enhancer elements. Genes Dev. 2: 1764.
54. Tanaka M., Lai J.-S., and Herr W. 1992. Promoter-selective activation domains in Oct-1 and Oct-2 direct differential activation of an snRNA and mRNA promoter. Cell 68: 755.
55. Triezenberg S.J., Kingsbury R.G., and McKnight S.L. 1988. Functional dissection of VP16, the trans-activator of herpes simplex virus immediate early gene expression. Genes Dev. 2: 718.
56. Walker S., Hayes S., and O'Hare P. 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.
57. Wilson A.C., Peterson M.G., and Herr W. 1995a. The HCF repeat is an unusual proteolytic cleavage signal. Genes Dev. 9: 2445.
58. Wilson A.C., LaMarco K., Peterson M.G., and Herr W. 1993. The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein. Cell 74: 115.
59. Wilson A.C., Freiman R.N., Goto H., Nishimoto T., and Herr W. 1997. VP16 targets an amino-terminal domain of HCF involved in cell cycle progression. Mol. Cell. Biol. 17: 6139.
60. Wilson A.C., Parrish J.E., Massa H.F., Nelson D.L., Trask B.J., and Herr W. 1995b. The gene encoding the VP16-accessory protein HCF (HCFC1) resides in human Xq28 and is highly expressed in fetal tissues and the adult kidney. Genomics 25: 462.
61. Xiao P. and Capone J.P. 1990. A cellular factor binds to the herpes simplex virus type 1 trans-activator Vmw65 and is required for Vmw65-dependent protein-DNA complex assembly with Oct-1. Mol. Cell. Biol. 10: 4974.