A single Cys sup 706 to Phe substitution in the retinoblastoma protein causes the loss of binding to SV40 T antigen
- Univ. of California, San Diego, La Jolla (United States)
- Univ. of California, San Francisco (United States)
- Univ. of Texas Health Science Center, San Antonio (United States)
Most naturally occurring mutants of the retinoblastoma (RB) protein contain large deletions or truncations. The small cell lung carcinoma cell line H209 contains a normal-sized but unphosphorylated RB protein, which fails to form a complex with SV40 T antigen, suggesting that the RB gene of H209 may contain a subtle mutation. To define this mutation, the RB complementary DNA and genomic DNA were sequenced, revealing a point mutation in exon 21 that changed a G to a T. This results in an amino acid substitution of a Phe for Cys{sup 706}. The mutant RB complementary DNA was used as a template for in vitro transcription and translation to synthesize the mutated protein. The resulting protein failed to bind to SV40 T antigen, demonstrating that a single missense mutation of the RB gene led to the complete inactivation of the ability of the RB protein to bind T antigen.
- OSTI ID:
- 7263194
- Journal Information:
- Cell Growth and Differentation; (United States), Vol. 1; ISSN 1044-9523
- Country of Publication:
- United States
- Language:
- English
Similar Records
A single amino acid substitution results in a retinoblastoma protein defective in phosphorylation and oncoprotein binding
Structure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domain
Related Subjects
LUNGS
CARCINOMAS
PROTEINS
BIOCHEMICAL REACTION KINETICS
GENE MUTATIONS
TUMOR CELLS
CELL PROLIFERATION
ANTIGENS
BIOLOGICAL FUNCTIONS
DNA SEQUENCING
TRANSCRIPTION
ANIMAL CELLS
BODY
DISEASES
KINETICS
MUTATIONS
NEOPLASMS
ORGANIC COMPOUNDS
ORGANS
REACTION KINETICS
RESPIRATORY SYSTEM
STRUCTURAL CHEMICAL ANALYSIS
550200* - Biochemistry
550900 - Pathology