Messenger and ribosomal RNA hydrolysis by ribonucleases I. The action of two barley leaf ribonucleases on the messenger and ribosomal RNA of isolated polysomes

Simpson R.S., Chakravorty A.K. and Scott K.J. (1980) Messenger and ribosomal RNA hydrolysis by ribonucleases I. The action of two barley leaf ribonucleases on the messenger and ribosomal RNA of isolated polysomes. Plant and Cell Physiology, 21 3: 413-423.

Author Simpson R.S.
Chakravorty A.K.
Scott K.J.
Title Messenger and ribosomal RNA hydrolysis by ribonucleases I. The action of two barley leaf ribonucleases on the messenger and ribosomal RNA of isolated polysomes
Journal name Plant and Cell Physiology   Check publisher's open access policy
ISSN 0032-0781
Publication date 1980-01-01
Sub-type Article (original research)
Volume 21
Issue 3
Start page 413
End page 423
Total pages 11
Subject 1804 Statistics, Probability and Uncertainty
2604 Applied Mathematics
2303 Ecology
1307 Cell Biology
1314 Physiology
1110 Nursing
Abstract When barley (Hordeum vulgare L.) leaf polysomes are incubated with two RNase fractions (the pH 5 insoluble and soluble RNases) under limit digestion conditions, the two enzymes exhibit characteristic preference for messenger and ribosomal RNA (mRNA and rRNA) hydrolysis. The pH 5 insoluble RNase from a cultivar of barley, Prior, and the corresponding enzyme from two near-isogenic lines (M1622 and M1623) cleave polysomal mRNA at specific sites and generate polysome profiles that are unique to the cultivar. By contrast, the soluble RNase from barley leaves, although a typical endoribonuclease, catalyzes no detectable hydrolysis of polysomal mRNA.Both of these barley leaf RNases hydrolyze rRNA when either polysomes or monosomes are treated with these enzymes. With polysomes as substrate, the pH 5 insoluble RNase hydrolyzes the high molecular weight RNA component of both large and small subunits of chloroplast and cytoplasmic ribosomes. The soluble RNase preferentially hydrolyzes the high molecular weight RNA component of the small subunit of chloroplast and cytoplasmic ribosomes. Analytical gel electrophoresis of the RNA of the RNase-treated monosomes has revealed that both enzymes hydrolyze rRNA into very small fragments. However, despite scission in rRNA at multiple sites, the RNase-treated monosomes remain active in polyuridylate-directed polyphenylalanine synthesis.
Keyword Chloroplast and cytoplasmic ribosomal subunits
Endoribonuclease
Hordeum vulgare L.
Limit digestion
Near-isogenic lines
Polyphenylalanine synthesis
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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Created: Tue, 23 Aug 2016, 11:14:56 EST by System User