HCF-1 amino- and carboxy-terminal subunit association through two separate sets of interaction modules: Involvement of fibronectin type 3 repeats

Wilson, A. C., Boutros, M., Johnson, K. M., Herr, W. (September 2000) HCF-1 amino- and carboxy-terminal subunit association through two separate sets of interaction modules: Involvement of fibronectin type 3 repeats. Molecular and Cellular Biology, 20 (18). pp. 6721-6730. ISSN 0270-7306

[img]
Preview
PDF (Paper)
Herr Mol Cell Biol 2000.pdf - Published Version

Download (643Kb) | Preview
URL: http://www.ncbi.nlm.nih.gov/pubmed/10958670
DOI: 10.1128/MCB.20.18.6721-6730.2000

Abstract

When herpes simplex virus infects permissive cells, the viral regulatory protein VP16 forms a specific complex with HCF-1, a preexisting nuclear protein involved in cell proliferation. The majority of HCF-1 in the cell is a complex of associated amino (BCF-1(N))- and carboxy (HCF-1(C))-terminal subunits that result from an unusual proteolytic processing of a large precursor polypeptide. Here, we have characterized the structure and function of sequences required for HCF-1(N) and HCF-1(C) subunit association. HCF-1 contains two matched pairs of self-association sequences called SAS1 and SAS2. One of these matched association sequences, SAS1, consists of a short 43-amino-acid region of the HCF-1(N) subunit, which associates with a carboxy-terminal region of the HCF-1(C) subunit that is composed of a tandem pair of fibronectin type 3 repeats, a structural motif known to promote protein-protein interactions. Unexpectedly, the related protein HCF-2, which is not proteolyzed, also contains a functional SAS1 association element, suggesting that this element does not function solely to maintain HCF-1(N) and HCF-1(C) subunit association. HCF-1(N) subunits do not possess a nuclear localization signal. We show that, owing to a carboxy-terminal HCF-1 nuclear localization signal, HCF-1(C) subunits can recruit HCF-1(N) subunits to the nucleus.

Item Type: Paper
Uncontrolled Keywords: HERPES-SIMPLEX VIRUS HOST-CELL FACTOR CRYSTAL-STRUCTURE NUCLEAR-LOCALIZATION PROTEIN HCF C1 FACTOR VP16 DOMAINS COMPLEX FAMILY
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
organism description > virus > herpes simplex virus
organism description > virus
CSHL Authors:
Communities: CSHL labs > Herr lab
Depositing User: Matt Covey
Date: September 2000
Date Deposited: 31 Jan 2014 14:36
Last Modified: 31 Jan 2014 14:36
PMCID: PMC86190
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29396

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving