Possible peptide chain termination mutants in thymide kinase gene of a mammalian virus, herpes simplex virus.
AUTOR(ES)
Summers, W P
RESUMO
Mutations in the viral gene coding for the thymidine kinase (ATP:thymidine 5'-phosphotransferase, EC 2.7.1.75) induced by herpes simplex virus have been obtained by selection of virus resistant to bromodeoxyuridine when grown in thymidine-kinase-deficient LMTK- mouse cells. Proteins labeled after infection of Vero (monkey) cells with herpes simplex virus were analyzed by gel electrophoresis and one protein of about 40,000 daltons was consistently altered in a number of thymidine-kinase-deficient mutants. Many viral mutants lacked this peptide and one class of these mutants induced the synthesis of new shorter peptides. Revertant virus could be selected which simultaneously regained the ability to induce thymidine kinase activity, regained the intact thymidine kinase peptide, and lost the ability to synthesize the shorter peptide fragment. These mutants comprise a class of animal virus mutants which have the properties expected of peptide chain termination mutants.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433142Documentos Relacionados
- Identification of new protein kinase-related genes in three herpesviruses, herpes simplex virus, varicella-zoster virus, and Epstein-Barr virus.
- In vitro suppression of UAG and UGA mutants in the thymidine kinase gene of herpes simplex virus.
- Identification of a common antigen of herpes simplex virus bovine herpes mammillitis virus, and B virus.
- In vitro transcription of the thymidine kinase gene of herpes simplex virus.
- Peptide Chain Termination with Mammalian Release Factor
