Accession Number : ADA265723


Title :   Cellular Mechanism of Turnover of the Stress Induced Protein HSP 70


Descriptive Note : Annual rept. 15 Apr 1992-14 Apr 1993


Corporate Author : WYOMING UNIV LARAMIE


Personal Author(s) : Petersen, Nancy


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a265723.pdf


Report Date : May 1993


Pagination or Media Count : 8


Abstract : Synthesis of the heat shock protein, hsp7O, appears to be essential for recovery from heat and chemical stress. Both because of the role of this protein in cellular recovery from stress and because of the possibility of using levels of hsp7O synthesis or accumulation as a measurement of cellular response in stress, it is important to study the stability of hsp7O. We have shown that Drosophila hsp7O decays in vitro by an autoproteolytic mechanism (Mitchell et al., 1985). Autoproteolytic decay could be part of the feedback mechanism regulating the levels of hsp7O accumulation if it occurs in vivo. To determine whether autoproteolytic decay is occurring in vivo, we propose to identify the in vivo breakdown products of hsp7O and to compare their N-terminal sequences to those of the in vitro breakdown products. Precisely the same cutting site would indicate that the same protease may be responsible for the decay in both cases. We will also determine the site of the protease activity in hsp7O for the in vitro decay


Descriptors :   *RECOVERY , *HEAT STRESS(PHYSIOLOGY) , MEASUREMENT , CHEMICALS , SITES , SEQUENCES , FEEDBACK , ACCUMULATION , SHOCK(PATHOLOGY) , PEPTIDE HYDROLASES , RELAXATION(PHYSIOLOGY) , DROSOPHILA , CUTTING , DECAY , HEAT , RESPONSE , SYNTHESIS(CHEMISTRY) , PROTEINS , STABILITY


Subject Categories : Biochemistry
      Stress Physiology


Distribution Statement : APPROVED FOR PUBLIC RELEASE