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Spontaneous Fragmentation of Several Proteins in Drosophila Pupae

Mitchell, Herschel K. and Petersen, Nancy S. (1987) Spontaneous Fragmentation of Several Proteins in Drosophila Pupae. Journal of Biological Chemistry, 262 (29). pp. 14298-14304. ISSN 0021-9258.

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Autoproteolysis is an essential activity in the expression of the entire genomes of a number of viruses. That is, new viruses can be produced only after large polyprotein products translated from the genome or from subgenomic mRNA degrade themselves to the polypeptides necessary for RNA replication or for the construction of new virus particles. We have recently shown that the major heat shock protein of Drosophila and a mouse cell line (70 kDa) also undergoes autoproteolysis with the production of specific patterns of smaller polypeptides. We show now that many other proteins in eucaryotic tissues also have a potential for self-degradation. We suggest that special coding regions in many genes may have important roles in both protein turnover and in the production of regulatory peptides.

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Additional Information:© 1987 American Society for Biochemistry and Molecular Biology. Received for publication, August 18, 1986, and in revised form, June 9, 1987. This work was supported by Public Health Service Grants GM25966B-06 and GM33602. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Funding AgencyGrant Number
Public Health ServiceGM25966B-06
Public Health ServiceGM33602
Issue or Number:29
Record Number:CaltechAUTHORS:20120626-101813358
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Official Citation:Spontaneous fragmentation of several proteins in Drosophila pupae. H K Mitchell and N S Petersen J. Biol. Chem. 1987 262: 14298-304
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:32090
Deposited By: Ruth Sustaita
Deposited On:26 Jun 2012 19:45
Last Modified:03 Oct 2019 03:57

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