Synthesis of trypanosome hsp70 mRNA is resistant to disruption of trans-splicing by heat shock.
Synthesis of mRNA in trypanosomes involves an apparent trans-splicing reaction whereby a common 39-nucleotide mini-exon sequence is joined to the protein-coding exon of a mRNA precursor. We have previously shown (Muhich, M. L., and Boothroyd, J. C. (1988) Mol. Cell. Biol. 8, 3837-3846) that the trans-splicing pathway of Trypanosoma brucei is sensitive to disruption by severe heat shock. Here we demonstrate that the synthesis of heat shock protein 70 (hsp 70) mRNA in T. brucei is apparently resistant to the heat-induced disruption of splicing. The 5'-ends of hsp 70 mRNAs are shown to be identical for molecules synthesized at either normal or heat shock temperatures, and in both cases, the 5'-terminal mini-exon sequence is present. These results suggest that T. brucei has evolved a mechanism which directly compensates for the deleterious effects of heat shock on trans-splicing, one which allows for the continued mini-exon-dependent trans-splicing of selected pre-mRNAs.
Muhich
M L
ML
Department of Microbiology and Immunology, Stanford University School of Medicine, California 94305-5402.
Boothroyd
J C
JC
D000818:Animals; D005091:Exons; D005786:Gene Expression Regulation; D006360:Heat-Shock Proteins / Q000235:genetics*; D006358:Hot Temperature; D012326:RNA Splicing; D012333:RNA, Messenger / Q000235:genetics*; D014346:Trypanosoma brucei brucei / Q000235:genetics*; D014404:Tubulin / Q000235:genetics
D006360:Heat-Shock Proteins; D012333:RNA, Messenger; D014404:Tubulin