NH2-terminal sequences of two src proteins that cause aberrant transformation.
AUTOR(ES)
Garber, E A
RESUMO
Two isolates of recovered avian sarcoma viruses (rASVs), rASV157 and rASV1702, transform cells in culture, but have greatly reduced in vivo tumorigenicity. The src proteins of rASV157 and rASV1702 have alterations within their NH2 termini, are not myristoylated, and have an altered subcellular localization. We have molecularly cloned and determined the nucleotide sequences of the src genes of rASV157 and rASV1702. We found that their src proteins have unusual NH2 termini: the rASV157 src protein NH2 terminus consists of 30 amino acids of the env signal peptide attached to Ser-6 of the src sequence, while the rASV1702 src protein NH2 terminus consists of 45 amino acids of the env signal peptide attached to Ala-76 of the src sequence. Expression of recombinant Rous sarcoma virus constructs containing the molecularly cloned rASV src genes produced src proteins with the same properties as those of the parental viruses. Our results suggest that the NH2-terminal structures are responsible for many unusual properties of the mutant src proteins.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=304145Documentos Relacionados
- Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation.
- NH2-Terminal Residues of Neurospora crassa Proteins
- Fine structural mapping of a critical NH2-terminal region of p60src.
- Tryptic peptide analysis and NH2-terminal amino acid sequences of polyhedrins of two baculoviruses from Orgyia pseudotsugata
- NH2-terminal amino acid sequence of human fibroblast interferon.