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Nucleic Acids Research, 1994, Vol. 22, No. 9 1640-1642
© 1994

MOLECULAR BIOLOGY

Heat shock-induced repression of proteolysis: poly(A)-binding protein degradation patterns can illusorily suggest its specific loss during heat shock

Valérie Lefrère1 and Roger F. Duncan1,*

Centre de Biologie du Developpement, Bat. IVR3, Universite Paul Sabatier 31062 Toulouse Cedex, France 1University of Southern California School of Pharmacy, Department of Molecular Pharmacology/Toxicology and School of Medicine, Department of Microbiology 1985 Zonal Avenue, Los Angeles, CA 90033, USA

*To whom correspondence should be addressed

Received January 21, 1994. Revised February 24, 1994. Accepted February 24, 1994.

Poly(A)-binding protein (PABP) is highly susceptible to proteolysis during cell lysis of Drosophila tissue culture cells unless substantial amounts of proteolysis inhibitors are included in the extraction buffer. This intrinsic proteolytic activity is substantially reduced during heat shock. An artifactual appearance that poly(A)-binding protein is specifically degraded by heat shock can result. Several contradictory descriptions of PABP may also be related to its proteolysis. Repression of proteolysis is likely to reflect a physiologically significant regulatory event, based on recent examinations of HSP70 stability during and after heat shock.


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O. P. d. M. Neto, J. A. Walker, C. M. d. Sa, and N. Standart
Levels of free PABP are limited by newly polyadenylated mRNA in early Spisula embryogenesis
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