Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae.
Open Access
- 1 February 1991
- journal article
- research article
- Published by Informa UK Limited in Molecular and Cellular Biology
- Vol. 11 (2), 1062-1068
- https://doi.org/10.1128/mcb.11.2.1062
Abstract
In the yeast Saccharomyces cerevisiae, the splicing of mRNA precursors is disrupted by a severe heat shock. Mild heat treatments prior to severe heat shock protect splicing from disruption, as was previously reported for Drosophila melanogaster. In contrast to D. melanogaster, protein synthesis during the pretreatment is not required to protect splicing in yeast cells. However, protein synthesis is required for the rapid recovery of splicing once it has been disrupted by a sudden severe heat shock. Mutations in two classes of yeast hsp genes affect the pattern of RNA splicing during the heat shock response. First, certain hsp70 mutants, which overproduce other heat shock proteins at normal temperatures, show constitutive protection of splicing at high temperatures and do not require pretreatment. Second, in hsp104 mutants, the recovery of RNA splicing after a severe heat shock is delayed compared with wild-type cells. These results indicate a greater degree of specialization in the protective functions of hsps than has previously been suspected. Some of the proteins (e.g., members of the hsp70 and hsp82 gene families) help to maintain normal cellular processes at higher temperatures. The particular function of hsp104, at least in splicing, is to facilitate recovery of the process once it has been disrupted.Keywords
This publication has 34 references indexed in Scilit:
- THE HEAT-SHOCK PROTEINSAnnual Review of Genetics, 1988
- Spliceosome assembly in yeast.Genes & Development, 1987
- Speculations on the functions of the major heat shock and glucose-regulated proteinsCell, 1986
- Hsp26 is not required for growth at high temperatures, nor for thermotolerance, spore development, or germinationCell, 1986
- RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesisCell, 1986
- Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growthCell, 1984
- hsp70: Nuclear concentration during environmental stress and cytoplasmic storage during recoveryCell, 1984
- A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene productNature, 1983
- Is the major Drosophila heat shock protein present in cells that have not been heat shocked?The Journal of cell biology, 1983
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970