Identification of functional regions in the transforming protein of Fujinami sarcoma virus by in-phase insertion mutagenesis
Identifieur interne : 001E45 ( Istex/Corpus ); précédent : 001E44; suivant : 001E46Identification of functional regions in the transforming protein of Fujinami sarcoma virus by in-phase insertion mutagenesis
Auteurs : James C. Stone ; Tom Atkinson ; Michael Smith ; Tony PawsonSource :
- Cell [ 0092-8674 ] ; 1984.
English descriptors
- Teeft :
- Agar, Amino acid residues, Catalytic domain, Cell lines, Cellular proteins, Cellular transformation, Central position, Coding sequence, Deletion, Digestion, England biolabs, Ethidium bromide, Experimental procedures, Fibroblast, Fibroblast transformation, Fujinami, Fujinami sarcoma virus, Functional domains, Functional regions, Further analysis, Further study, Genome, Hanafusa, Insertion, Insertion mutagenesis, Insertion mutants, Insertion mutations, Kinase, Kinase activity, Kinase reaction, Linear molecules, Linker, Linker deletion, Linker mutations, Local disruption, Locus, Mammalian cells, Medical research council, Monolinker mutation, Morphological transformation, Mutagenesis, Mutant, Mutation, National cancer institute, Nucleotide sequence, Oncogene, Oncogene product, Peptide insertion, Personal communication, Phosphorylation, Plasmid, Primary structure, Protein kinase activity, Reading frame, Recognition sequence, Regular medium, Restriction sites, Rous sarcoma virus, Sarcoma, Shibuya, Small colonies, Soft agar, Thymidine kinase gene, Transfection, Transfection experiments, Viral, Viral protein.
Abstract
Abstract: A novel mutagenesis procedure based on the insertion of a hexameric nucleotide sequence into Rsa I restriction sites of cloned DNA has been applied to a copy of the Fujinami sarcoma virus (FSV) genome with the aim of identifying functional regions in the transforming protein. Mutations specifying peptide insertions in both the NH2- and the COOH-terminal fps-specific portions of the transforming protein reduce or abolish the capacity of the genome to induce transformed foci in rat-2 cells. Insertion of multiple copies of the hexamer into one central position in the oncogene results in dislocation of the NH2- and COOH-terminal regions in the primary structure, but has no inhibitory effect on focus induction. Taken together, the results imply that both the NH2- and COOH-terminal fps-specific portions of the FSV oncogene product possess determinants which function in fibroblast transformation, and that cooperation of these two regions is not sensitive to their separation in the primary structure.
Url:
DOI: 10.1016/0092-8674(84)90385-4
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Abstract: A novel mutagenesis procedure based on the insertion of a hexameric nucleotide sequence into Rsa I restriction sites of cloned DNA has been applied to a copy of the Fujinami sarcoma virus (FSV) genome with the aim of identifying functional regions in the transforming protein. Mutations specifying peptide insertions in both the NH2- and the COOH-terminal fps-specific portions of the transforming protein reduce or abolish the capacity of the genome to induce transformed foci in rat-2 cells. Insertion of multiple copies of the hexamer into one central position in the oncogene results in dislocation of the NH2- and COOH-terminal regions in the primary structure, but has no inhibitory effect on focus induction. Taken together, the results imply that both the NH2- and COOH-terminal fps-specific portions of the FSV oncogene product possess determinants which function in fibroblast transformation, and that cooperation of these two regions is not sensitive to their separation in the primary structure.</div>
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<abstract xml:lang="en"><p>Abstract: A novel mutagenesis procedure based on the insertion of a hexameric nucleotide sequence into Rsa I restriction sites of cloned DNA has been applied to a copy of the Fujinami sarcoma virus (FSV) genome with the aim of identifying functional regions in the transforming protein. Mutations specifying peptide insertions in both the NH2- and the COOH-terminal fps-specific portions of the transforming protein reduce or abolish the capacity of the genome to induce transformed foci in rat-2 cells. Insertion of multiple copies of the hexamer into one central position in the oncogene results in dislocation of the NH2- and COOH-terminal regions in the primary structure, but has no inhibitory effect on focus induction. Taken together, the results imply that both the NH2- and COOH-terminal fps-specific portions of the FSV oncogene product possess determinants which function in fibroblast transformation, and that cooperation of these two regions is not sensitive to their separation in the primary structure.</p>
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<abstract lang="en">Abstract: A novel mutagenesis procedure based on the insertion of a hexameric nucleotide sequence into Rsa I restriction sites of cloned DNA has been applied to a copy of the Fujinami sarcoma virus (FSV) genome with the aim of identifying functional regions in the transforming protein. Mutations specifying peptide insertions in both the NH2- and the COOH-terminal fps-specific portions of the transforming protein reduce or abolish the capacity of the genome to induce transformed foci in rat-2 cells. Insertion of multiple copies of the hexamer into one central position in the oncogene results in dislocation of the NH2- and COOH-terminal regions in the primary structure, but has no inhibitory effect on focus induction. Taken together, the results imply that both the NH2- and COOH-terminal fps-specific portions of the FSV oncogene product possess determinants which function in fibroblast transformation, and that cooperation of these two regions is not sensitive to their separation in the primary structure.</abstract>
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