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Phorbol ester binding to protein kinase C requires a cysteine-rich zinc-finger-like sequence

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
Protein kinase C normally has a tandem repeat of a characteristic cysteine-rich sequence in C{sub 1}, the conserved region of the regulatory domain. These sequences resemble the DNA-binding zinc finger domain. For the {gamma} subspecies of rat brain protein kinase C, various deletion and point mutants in this domain were constructed, and the mutated proteins were expressed in Escherichia coli by using the T7 expression system. Radioactive phorbol 12,13-dibutyrate binding analysis indicated that a cysteine-rich zinc-finger-like sequence was essential for protein kinase C to bind phorbol ester and that one of the two sequences was sufficient for the phorbol ester binding. Conserved region C{sub 2}, another region in the regulatory domain, was apparently needed for the enzyme to require Ca{sup 2+} for phorbol ester binding activity.
OSTI ID:
5300110
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 86:13; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English