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J. Biol. Chem., Vol. 255, Issue 16, 7529-7532, Aug, 1980
KD Wilkinson, MK Urban and AL Haas
A small heat-stable polypeptide, ATP-dependent proteolysis factor 1
(APF-1), is an essential component of the ATP-dependent proteolytic system
of rabbit reticulocytes (Ciechanover, A., Hod, Y., and Hershko. A. (1978)
Biochem. Biophys. Res Commun. 81, 1100-1105). The following evidence
supports the view that APF-1 is ubiquitin, a highly conserved heat-stable
polypeptide found universally in nature: 1) APF-1 and ubiquitin (generously
given by G. Goldstein) yield co-migrating bands on five polyacrylamide gel
electrophoresis systems and in isoelectric focusing; 2) amino acid analysis
shows excellent agreement between the two proteins; 3) APF-1 and ubiquitin
give similar specific activity, in activating the ATP-dependent proteolysis
system; 4) 125I-APF-1 and 125I- ubiquitin form electrophoretically
identical covalent conjugates with endogenous reticulocyte proteins.
Recently, such conjugates have been proposed as the active intermediates in
ATP-dependent proteolysis (Ciechanover, A., Heller, H., Hershko, A., Haas,
A.L., and Rose, I.A. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 1783-1786).
Thus, ubiquitin is an essential component of the ATP-dependent system in
reticulocytes and a similar role in degradation and proteolytic processing
in other cells is likely.
Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes
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