VP16 Targets an Amino-Terminal Domain of HCF Involved in Cell Cycle Progression

REFERENCES

• Alexandre, C., D. A. Grueneberg, and M. Z. Gilman. 1993. Studying heterologous transcription factors in yeast. Methods 5:147–155.
   Google Scholar
• Boeke, J. D., J. Trueheart, G. Natsoulis, and G. R. Fink. 1987. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154:164–175.
   PubMed Web of Science ®Google Scholar
• Bork, P., and R. F. Doolittle. 1994. Drosophila kelch motif is derived from a common enzyme fold. J. Mol. Biol. 236:1277–1282.
   PubMedGoogle Scholar
• Branden, C., and J. Tooze. 1991. Introduction to protein structure. Garland Inc., New York, N.Y.
   Google Scholar
• Chong, J. A., J. Tapia-Ramirez, S. Kim, J. J. Toledo-Aral, Y. Zheng, M. C. Boutros, Y. M. Altshuller, M. A. Frohman, S. D. Kraner, and G. Mandel. 1995. REST: a mammalian silencer protein that restricts sodium channel gene expression to neurons. Cell 80:949–957.
   PubMed Web of Science ®Google Scholar
• Clapham, D. E. 1996. The G-protein nanomachine. Nature 379:297–299.
   PubMedGoogle Scholar
• Cleary, M. A., S. Stern, M. Tanaka, and W. Herr. 1993. Differential positive control by Oct-1 and Oct-2: activation of a transcriptionally silent motif through Oct-1 and VP16 corecruitment. Genes Dev. 7:72–83.
   PubMedGoogle Scholar
• Eichinger, L., L. Bomblies, J. Vandekerckhove, M. Schleicher, and J. Gettemans. 1996. A novel type of protein kinase phosphorylates actin in the actin-fragmin complex. EMBO J. 15:5547–5556.
   PubMedGoogle Scholar
• Frattini, A., A. Chatterjee, S. Faranda, M. G. Sacco, A. Villa, G. E. Herman, and P. Vezzoni. 1996. The chromosome localization and the HCF repeats of the human host cell factor gene (HCFC1) are conserved in the mouse homologue. Genomics 32:277–280.
   PubMedGoogle Scholar
• Freiman, R. N., A. C. Wilson, and W. Herr. Unpublished results.
   Google Scholar
• Gerster, T., and R. G. Roeder. 1988. A herpesvirus transactivator protein interacts with transcription factor OTF-1 and other cellular proteins. Proc. Natl. Acad. Sci. USA 85:6347–6351.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Ito, N., S. E. V. Phillips, K. D. S. Yadav, and P. F. Knowles. 1994. Crystal structure of a free radical enzyme, galactose oxidase. J. Mol. Biol. 238:794–814.
   PubMed Web of Science ®Google Scholar
• Katan, M., A. Haigh, C. P. Verrijzer, P. C. Van der Vliet, and P. O’Hare. 1990. Characterization of a cellular factor which interacts functionally with Oct-1 in the assembly of a multicomponent transcription complex. Nucleic Acids Res. 18:6871–6880.
   PubMedGoogle Scholar
• Kristie, T. M., J. H. LeBowitz, and P. A. Sharp. 1989. The octamer-binding proteins form multi-protein-DNA complexes with the HSV aTIF regulatory protein. EMBO J. 8:4229–4238.
   PubMedGoogle Scholar
• Kristie, T. M., J. L. Pomerantz, T. C. Twomwey, 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.
   PubMedGoogle Scholar
• Kristie, T. M., and P. A. Sharp. 1990. Interactions of the Oct-1 POU subdomains with specific DNA sequences and with the HSV a-trans-activator protein. Genes Dev. 4:2383–2396.
   PubMedGoogle Scholar
• Kristie, T. M., and P. A. Sharp. 1993. Purification of the cellular C1 factor required for the stable recognition of the Oct-1 homeodomain by the herpes simplex virus a-trans-induction factor (VP16). J. Biol. Chem. 268:6525–6534.
   PubMedGoogle Scholar
• 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.
   PubMedGoogle Scholar
• Lai, J.-S., and W. Herr. 1992. Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations. Proc. Natl. Acad. Sci. USA 89:6958–6962.
   PubMed Web of Science ®Google Scholar
• Lai, J.-S., and W. Herr. 1997. Interdigitated residues within a small region of VP16 interact with Oct-1, host cell factor, and DNA. Mol. Cell. Biol. 17:3937–3946.
   PubMedGoogle Scholar
• Lambright, D. G., J. Sondek, A. Bohm, N. P. Skiba, H. E. Hamm, and P. B. Sigler. 1996. The 2.0 Å crystal structure of a heterotrimeric G protein. Nature 379:311–319.
   PubMed Web of Science ®Google Scholar
• Murzin, A. G., A. M. Lesk, and C. Chothia. 1994. Principles determining the structure of beta-sheet barrels in proteins. II. The observed structures. J. Mol. Biol. 236:1382–1400.
   PubMedGoogle Scholar
• Nishimoto, T., and C. Basilico. 1978. Analysis of a method for selecting temperature sensitive mutants of BHK cells. Somatic Cell Genet. 4:323–340.
   PubMedGoogle Scholar
• O’Hare, P. 1993. The virion transactivator of herpes simplex virus. Semin. Virol. 4:145–155.
   Google Scholar
• 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.
   PubMedGoogle Scholar
• 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.
   PubMedGoogle Scholar
• Sondek, J., A. Bohm, D. G. Lambright, H. E. Hamm, and P. B. Sigler. 1996. Crystal structure of a GA protein þμ dimer at 2.1 Å resolution. Nature 379:369–374.
   PubMed Web of Science ®Google Scholar
• Springer, T. A. 1997. Folding of the N-terminal, ligand-binding region of integrin a-subunits into a þ-propeller domain. Proc. Natl. Acad. Sci. USA 94:65–72.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Tanaka, M., J.-S. Lai, and W. Herr. 1992. Promoter-selective activation domains in Oct-1 and Oct-2 direct differential activation of an snRNA and mRNA promoter. Cell 68:755–767.
   PubMed Web of Science ®Google Scholar
• Thomas, B. J., and R. Rothstein. 1989. Elevated recombination rates in transcriptionally active DNA. Cell 56:619–630.
   PubMed Web of Science ®Google Scholar
• Thompson, C. C., and S. L. McKnight. 1992. Anatomy of an enhancer. Trends Genet. 8:232–236.
   Google Scholar
• Varghese, J. N., W. G. Laver, and P. M. Colman. 1983. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature 303:35–40.
   PubMed Web of Science ®Google Scholar
• Varkey, J. P., P. J. Muhlrad, A. N. Minniti, B. Do, and S. Ward. 1995. The Caenorhabditis elegans spe-26 gene is necessary to form spermatids and encodes a protein similar to the actin-associated proteins kelch and scruin. Genes Dev. 9:1074–1086.
   PubMedGoogle Scholar
• Wall, M. A., D. E. Coleman, E. Lee, J. A. Iniguez-Lluhi, B. A. Posner, A. G. Gilman, and S. R. Sprang. 1995. The structure of the G protein heterotrimer Gia1þ1μ2. Cell 83:1047–1058.
   PubMed Web of Science ®Google Scholar
• Watanabe, M., N. Furuno, M. Goebl, M. Go, K. Miyauchi, T. Sekiguchi, C. Basilico, and T. Nishimoto. 1991. Molecular cloning of the human gene, CCG2, that complements the BHK-derived thermosensitive cell cycle mutant tsBN63: identity of CCG2 with the human X chromosomal SCAR/ RPS4X gene. J. Cell Sci. 100:35–43.
   PubMedGoogle Scholar
• Way, M., M. Sanders, C. Garcia, J. Sakai, and P. Matsudaira. 1995. Sequence and domain organization of scruin, and actin-crosslinking protein in the acrosomal process of Limulus sperm. J. Cell Biol. 128:51–60.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Wilson, A. C., M. A. Cleary, J.-S. Lai, K. LaMarco, M. G. Peterson, and W. Herr. 1993. Combinatorial control of transcription: the herpes simplex virus VP16-induced complex. Cold Spring Harbor Symp. Quant. Biol. 58:167–178.
   PubMedGoogle Scholar
• Wilson, A. C., M. G. Peterson, and W. Herr. 1995. The HCF repeat is an unusual proteolytic cleavage signal. Genes Dev. 9:2445–2458.
   PubMed Web of Science ®Google Scholar
• Wilson, A. C., and W. Herr. Unpublished results.
   Google Scholar
• Xia, Z.-X., W.-W. Dai, J.-P. Xiong, Z.-P. Hao, V. L. Davidson, S. White, and S. F. Mathews. 1992. The three-dimensional structure of methanol dehydrogenase from two methylotrophic bacteria at 2.6-Å resolution. J. Biol. Chem. 267:22289–22297.
   PubMed Web of Science ®Google Scholar
• Xiao, P., and J. P. Capone. 1990. A cellular factor binds to the herpes simplex virus type 1 transactivator Vmw65 and is required for Vmw65-dependent protein-DNA complex assembly with Oct-1. Mol. Cell Biol. 10:4974–4977.
   PubMedGoogle Scholar
• Xue, F., and L. Cooley. 1993. Kelch encodes a component of intercellular bridges in Drosophila egg chambers. Cell 72:681–693.
   PubMed Web of Science ®Google Scholar