Abstract:
:It had been shown previously that the heat-stable polypeptide of the ATP-dependent proteolytic system of reticulocytes, designated APF-1, forms covalent conjugates with protein substrates in an ATP-requiring process. We now describe an enzyme that carries out the activation by ATP of the polypeptide with pyrophosphate displacement. The formation of AMP-polypeptide and transfer of the polypeptide to a secondary acceptor are suggested by an APF-1 requirement for ATP-PPi and ATP-AMP exchange reactions, respectively. With radiolabeled polypeptide, an ATP-dependent labeling of the enzyme was shown to be by a linkage that is acid stable but is labile to treatment with mild alkali, hydroxylamine, borohydride, or mercuric salts. It therefore appears that the AMP-polypeptide undergoes attack by an -SH group of the enzyme to form a thiolester.
journal_name
Proc Natl Acad Sci U S Aauthors
Ciechanover A,Heller H,Katz-Etzion R,Hershko Adoi
10.1073/pnas.78.2.761subject
Has Abstractpub_date
1981-02-01 00:00:00pages
761-5issue
2eissn
0027-8424issn
1091-6490journal_volume
78pub_type
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