The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16

Stern, S., Tanaka, M., Herr, W. (October 1989) The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16. Nature, 341 (6243). pp. 624-30. ISSN 1476-4687

URL: http://www.ncbi.nlm.nih.gov/pubmed/2571937
DOI: 10.1038/341624a0

Abstract

The herpes simplex virus transactivator VP16 participates in the formation of a multiprotein-DNA complex with the ubiquitous octamer-motif-binding factor Oct-1. Complex formation is dependent on specific amino acids in the Oct-1 homoeodomain which are in positions analogous to positive control mutations in helix 2 of the lambda phage repressor helix-turn-helix motif, indicating that this structure is an ancient target for protein-protein interactions mediating transcriptional control.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence DNA-Binding Proteins/*metabolism/*physiology *Gene Expression Regulation, Viral *Genes, Homeobox Macromolecular Substances Molecular Sequence Data Multiprotein Complexes Phosphoproteins/*metabolism Protein Binding Protein Conformation Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Simplexvirus/*genetics Structure-Activity Relationship Trans-Activators/*metabolism Transcription Factors/*metabolism/*physiology/ultrastructure
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
organism description > virus > herpes simplex virus
CSHL Authors:
Communities: CSHL labs > Herr lab
Depositing User: Gail Sherman
Date: 19 October 1989
Date Deposited: 23 Jun 2017 19:28
Last Modified: 23 Jun 2017 19:28
Related URLs:
URI: http://repository.cshl.edu/id/eprint/34910

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