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PMID: 3485284 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Heat shock causes destabilization of specific mRNAs and destruction of endoplasmic reticulum in barley aleurone cells.

Belanger FC, Brodl MR, Ho TH

Abstract

In response to a phytohormone, gibberellic acid, the aleurone layers of barley seeds synthesize and secrete alpha-amylases, which are coded by a set of stable mRNAs. When aleurone layers are subjected to heat shock treatment, the synthesis of alpha-amylase is suppressed while heat shock proteins are induced. The suppression of alpha-amylase synthesis is not the result of translational control as reported in several other systems. Rather, the sequences of alpha-amylase mRNA are rapidly degraded during heat shock as shown by in vitro translation and dot blot hybridization with a cDNA probe. Upon recovery from heat shock, the tissue resumes the synthesis of alpha-amylase in 2-4 hr. However, in the presence of a transcription inhibitor, cordycepin, the resumption of synthesis of alpha-amylase does not take place, indicating that new transcription of alpha-amylase genes is necessary for this recovery process. The degradation of alpha-amylase mRNAs correlates with the rapid destruction of endoplasmic reticulum as observed by electron microscopy, a phenomenon that has not been reported previously as a heat shock response. Since alpha-amylase mRNA is associated with the endoplasmic reticulum via membrane-bound polyribosomes, we suggest that the destruction of the endoplasmic reticulum during heat shock causes the destabilization and the eventual degradation of alpha-amylase mRNA.

MeSH Terms
Deoxyadenosines/pharmacology Endoplasmic Reticulum/ultrastructure Enzyme Induction/drug effects Gibberellins/pharmacology Heat-Shock Proteins/genetics Hordeum/cytology,metabolism Hot Temperature RNA, Messenger/metabolism Time Factors Transcription, Genetic alpha-Amylases/genetics,metabolism
Chemicals
Deoxyadenosines Gibberellins Heat-Shock Proteins RNA, Messenger gibberellic acid alpha-Amylases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Belanger F C
Brodl M R
Ho T H
References (21)
21 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1986-03-00
Pages
1354-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC323074
Subset
IM
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