Transcriptional and translational analysis of the murine 84- and 86-kDa heat shock proteins.

摘要: Abstract The mammalian 85-90-kDa heat shock protein(s) (hsp) have been shown to exist as two species of 84 and 86 kDa (Ullrich, S. J., Robinson, E. A., Law, L. W., Willingham, M., Appella, (1986) Proc. Natl. Acad. Sci. U. A. 83, 3121-3125). Two cDNA clones corresponding the forms isolated which specifically hybridize either a 2.85- or 3.0-kilobase pair transcript hsp 86, respectively (Moore, K., Kozak, C., Ullrich, (1987) Gene (Amst.) 56, 29-40, this paper). regulation these were examined in nontransformed NIH-3T3 chemically transformed Meth A cells. basal level mRNA was approximately 2.5-fold greater than transcript, with ratio protein synthesis 2.5:1. After transient (10 min, 44 degrees C), rate transcription increased 4.5- 7-fold, respectively, within 0.5 h remained elevated for 2 h. Northern blot analysis performed on cells, during recovery from shock, indicated that both cells levels rapidly, peaking at 5 post-heat shock; transcripts 1.5- 2-fold higher non-heat-shocked respectively. after correlated each cell lines. In mRNA, synthesis, steady state vitro 2-3-fold tumors vivo, reduced compared levels. Thus, normal murine are heat-inducible, transcriptionally translationally, expressing 86. data suggest syntheses primarily regulated.