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Negative charge at the casein kinase II phosphorylation site is important for transformation but not for Rb protein binding by the E7 protein of human papillomavirus type 16.

Firzlaff, J M and Lüscher, B and Eisenman, R N (1991) Negative charge at the casein kinase II phosphorylation site is important for transformation but not for Rb protein binding by the E7 protein of human papillomavirus type 16. Proceedings of the National Academy of Sciences of the United States of America, 88 (12). pp. 5187-5191. ISSN 0027-8424

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Article URL: http://www.pnas.org/content/88/12/5187.full.pdf

Abstract

The human papillomavirus E7 protein is phosphorylated at the two serines in positions 31/32, which are part of a consensus sequence for casein kinase II (CKII). In this study, we have investigated the effect of CKII phosphorylation site mutations, all of which lead to unphosphorylated E7 proteins. The replacement of the two serines by uncharged alanine residues drastically reduced the ability of E7 to cotransform primary cells with ras, whereas negatively charged aspartic acid at the same positions produced only a slight effect. This difference was not reflected in the p105Rb binding or the E2 promoter transactivation capability of these two mutants. Mutations that changed the CKII consensus without altering the serine residues also resulted in a loss of phosphorylation and transformation. This indicated that negative charge at positions 31/32 provided either by phosphorylation or by a negatively charged amino acid is necessary for efficient transformation without significantly affecting p105Rb binding or transactivation.

Item Type: Article
Additional Information: This article is freely available in PubMed Central and at the journal's website.
PubMed ID: 2052600
PMCID: PMC51837
Grant Numbers: PO1CA28151
Keywords or MeSH Headings: Adenoviridae/genetics; Amino Acid Sequence; Base Sequence; Binding Sites; Casein Kinases; Genes, Viral; Humans; Molecular Sequence Data; Mutation; Oncogene Proteins, Viral/metabolism; Open Reading Frames; Phosphorylation; Precipitin Tests; Promoter Regions (Genetics); Protein Kinases/genetics/metabolism; Retinoblastoma Protein/metabolism; Trans-Activation (Genetics); Transfection; Transformation, Genetic;
Subjects: Cellular and Organismal Processes > Genetic processes > Mutation
Molecules > Molecular structure
Molecules > Proteins
Molecules > Genes > Oncogenes
Depositing User: Library Staff
Date Deposited: 03 Dec 2008 20:58
Last Modified: 21 May 2010 22:54
URI: http://authors.fhcrc.org/id/eprint/134

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