PMID- 3660586 OWN - NLM STAT- MEDLINE DCOM- 19871109 LR - 20190714 IS - 0042-6822 (Print) IS - 0042-6822 (Linking) VI - 160 IP - 2 DP - 1987 Oct TI - Identification of an amino terminal domain required for the transforming activity of the Rous sarcoma virus src protein. PG - 400-10 AB - Transformation of chicken cells by Rous sarcoma virus (RSV) requires the functional expression of the viral src protein, a tyrosine protein kinase, pp60src. Variants of RSV containing deletions within the amino terminal one-third of the src protein have been identified that exhibit either temperature-sensitive or transformation-defective phenotype when used to infect chicken embryo cells. To define the regions within the amino terminal portion of pp60src that influence morphological transformation, a series of overlapping deletion mutations in the src gene of Prague A RSV (Pr A RSV) were constructed and their biological and biochemical properties were analyzed. Deletions within the src gene which remove amino acid residues 38 to 142 had minimal effects on the ability of the mutant viruses to induce cellular transformation. However, deletions, which impinged upon the region of the src gene encoding residues 142 to 169, inhibited cellular transformation. A variant containing a deletion of amino acid residues 169 to 225, was temperature sensitive for transformation. Structurally altered src proteins recovered from cells infected with transformation-defective variants exhibited a somewhat reduced tyrosine protein kinase activities when assayed in the immune complex kinase assay. Analysis of the in vivo phosphorylation of a pp60src substrate, the 36-kDa protein, revealed virtually wild-type levels of phosphorylation in cells infected with the transformation-defective mutants. These studies suggest that the region of the Pr A RSV src protein delineated by amino acid residues 142 to 169 is essential for initiation and maintenance of morphological transformation of chicken cells in culture. FAU - Raymond, V W AU - Raymond VW AD - Department of Microbiology, University of Virginia School of Medicine, Charlottesville 22908. FAU - Parsons, J T AU - Parsons JT LA - eng GR - CA27578/CA/NCI NIH HHS/United States GR - CA29243/CA/NCI NIH HHS/United States PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, P.H.S. PL - United States TA - Virology JT - Virology JID - 0110674 RN - 0 (Oncogene Proteins, Viral) RN - 0 (Phosphoproteins) RN - EC 2.7.10.1 (Protein-Tyrosine Kinases) SB - IM MH - Amino Acid Sequence MH - Animals MH - *Cell Transformation, Viral MH - Cells, Cultured MH - Chick Embryo MH - Chromosome Deletion MH - Mutation MH - Oncogene Proteins, Viral/*physiology MH - *Oncogenes MH - Peptide Mapping MH - Phosphoproteins/metabolism MH - Protein-Tyrosine Kinases/metabolism MH - Structure-Activity Relationship EDAT- 1987/10/01 00:00 MHDA- 1987/10/01 00:01 CRDT- 1987/10/01 00:00 PHST- 1987/10/01 00:00 [pubmed] PHST- 1987/10/01 00:01 [medline] PHST- 1987/10/01 00:00 [entrez] AID - 10.1016/0042-6822(87)90011-0 [doi] PST - ppublish SO - Virology. 1987 Oct;160(2):400-10. doi: 10.1016/0042-6822(87)90011-0.