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PMID: 6769112 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 77 ·No. 3 ·1980-03-00 ·Pages 1365-8

Ciechanover A, Heller H, Elias S, Haas AL, Hershko A

Abstract

The heat-stable polypeptide (APF-1) required for ATP-dependent proteolysis in reticulocytes enters into high molecular weight conjugates upon incubation with the fraction of reticulocytes that is retained by DEAE-cellulose. Conjugate formation requires ATP and Mg2+ and its inhibited by N-ethylmaleimide. UTP and GTP are inactive. These properties are identical to those of ATP-dependent protein breakdown in the same system, suggesting that the conjugates are intermediates in this process. The APF-1 conjugates are stable in sodium dodecyl sulfate/polyacrylamide gel electrophoresis and Sephadex G-75 isolation and are resistant to mild acid, alkali, heat denaturation, and reduction; the conjugates are therefore covalent.

MeSH Terms
Adenosine Triphosphate/metabolism Animals Edetic Acid/pharmacology Ethylmaleimide/pharmacology Hydrogen-Ion Concentration Kinetics Peptide Hydrolases/metabolism Protein Binding/drug effects Proteins/metabolism Rabbits Reticulocytes/metabolism Ribonucleotides/pharmacology
Chemicals
Proteins Ribonucleotides Adenosine Triphosphate Edetic Acid Peptide Hydrolases Ethylmaleimide
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ciechanover A
Heller H
Elias S
Haas A L
Hershko A
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16 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.77.3.1365
Published
1980-03-00
Pages
1365-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC348495
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.77.3.1365 PMC Full Text View journal details
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