Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein

The transforming protein of Rous sarcoma virus, p60src, was shown to be acylated at its amino terminus with the long-chain fatty acid myristic acid by isolation of a tryptic peptide with the following structure: myristylglycylserylseryllysine. The occurrence of this unusual posttranslational modific...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 1985-01, Vol.227 (4685), p.427-429
Hauptverfasser: Schultz, A.M, Henderson, L.E, Oroszlan, S, Garber, E.A, Hanafusa, H
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Sprache:eng
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Zusammenfassung:The transforming protein of Rous sarcoma virus, p60src, was shown to be acylated at its amino terminus with the long-chain fatty acid myristic acid by isolation of a tryptic peptide with the following structure: myristylglycylserylseryllysine. The occurrence of this unusual posttranslational modification in the cyclic adenosine monophosphate-dependent protein kinase and in several transforming protein kinases of mammalian retroviruses suggests that myristylation of the amino terminal glycyl residue may be critical for the function of certain proteins related to cell transformation and growth control.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.3917576