PMID- 10629049 OWN - NLM STAT- MEDLINE DCOM- 20000214 LR - 20210526 IS - 0270-7306 (Print) IS - 0270-7306 (Linking) VI - 20 IP - 3 DP - 2000 Feb TI - Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP. PG - 919-28 AB - Host cell factor 1 (HCF-1) is a nuclear protein required for progression through G(1) phase of the cell cycle and, via its association with VP16, transcriptional activation of the herpes simplex virus immediate-early genes. Both functions require a six-bladed beta-propeller domain encoded by residues 1 to 380 of HCF-1 as well as an additional amino-terminal region. The beta-propeller domain is well conserved in HCF homologues, consistent with a critical cellular function. To date, the only known cellular target of the beta-propeller is a bZIP transcription factor known as LZIP or Luman. Whether the interaction between HCF-1 and LZIP is required for cell proliferation remains to be determined. In this study, we used directed mutations to show that all six blades of the HCF-1 beta-propeller contribute to VP16-induced complex assembly, association with LZIP, and cell cycle progression. Although LZIP and VP16 share a common tetrapeptide HCF-binding motif, our results reveal profound differences in their interaction with HCF-1. Importantly, with several of the mutants we observe a poor correlation between the ability to associate with LZIP and promote cell proliferation in the context of the full HCF-1 amino terminus, arguing that the HCF-1 beta-propeller domain must target other cellular transcription factors in order to contribute to G(1) progression. FAU - Mahajan, S S AU - Mahajan SS AD - Department of Microbiology, Kaplan Comprehensive Cancer Center, New York University School of Medicine, New York, New York 10016, USA. FAU - Wilson, A C AU - Wilson AC LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - United States TA - Mol Cell Biol JT - Molecular and cellular biology JID - 8109087 RN - 0 (CREB3 protein, human) RN - 0 (Cyclic AMP Response Element-Binding Protein) RN - 0 (HCFC1 protein, human) RN - 0 (Herpes Simplex Virus Protein Vmw65) RN - 0 (Host Cell Factor C1) RN - 0 (Proteins) RN - 0 (Recombinant Proteins) RN - 0 (Transcription Factors) SB - IM MH - Amino Acid Sequence MH - Amino Acid Substitution MH - Cell Cycle/*physiology MH - Cell Division MH - Cell Line MH - Cyclic AMP Response Element-Binding Protein MH - G1 Phase MH - Herpes Simplex Virus Protein Vmw65/*metabolism MH - Host Cell Factor C1 MH - Humans MH - Leucine Zippers MH - Molecular Sequence Data MH - Mutagenesis, Site-Directed MH - Protein Structure, Secondary MH - Proteins/chemistry/*genetics/*metabolism MH - Recombinant Proteins/chemistry/metabolism MH - Repetitive Sequences, Amino Acid MH - Sequence Alignment MH - Sequence Homology, Amino Acid MH - Simplexvirus/*genetics/metabolism MH - Transcription Factors/*metabolism MH - Transfection PMC - PMC85209 EDAT- 2000/01/11 09:00 MHDA- 2000/02/19 09:00 CRDT- 2000/01/11 09:00 PHST- 2000/01/11 09:00 [pubmed] PHST- 2000/02/19 09:00 [medline] PHST- 2000/01/11 09:00 [entrez] AID - 10.1128/MCB.20.3.919-928.2000 [doi] PST - ppublish SO - Mol Cell Biol. 2000 Feb;20(3):919-28. doi: 10.1128/MCB.20.3.919-928.2000.