Interplay among processing and degradative enzymes and a precursor ribonucleic acid in the selective maturation and maintenance of ribonucleic acid molecules
- 16 August 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 22 (17), 4000-4005
- https://doi.org/10.1021/bi00286a002
Abstract
In order to understand why the 1st tRNA (tRNAGln) in the T4 tRNA gene cluster is not produced when T4 infects an RNase III- mutant of Escherichia coli, RNA metabolism was analyzed in RNase III- RNAse P- (rnc, rnp) cells infected with phage T4. After such an infection a new dimeric precursor RNA molecule of tRNAGln and tRNALeu was identified and analyzed. This molecule is structurally very simliar to K band RNA that accumulates in rnc+ rnp strains. It is 4 nucleotides shorter than K RNA at the 5'' end. The molecule, like K RNA, contains 2 RNase P processing sites at the 5'' ends of each tRNA. Both sites are accessible to RNase P. While in the K RNA the site at the 5'' end of tRNALeu (the site in the middle of the substrate) is more efficiently cleaved than the other site, this differential is even increased in the Ks (K-like) molecule). This difference is sufficiently large that in vivo in the RNase III- strain the smaller precursor of tRNAGln is degraded rather than being matured to tRNAGln by RNase P. This information contributes to the elucidation of the key role of RNase III in the processing of T4 tRNA. It shows the dependence of RNase P activity at the 5'' end of tRNAGln on a correct and specific cleavage by RNase III at a position 6 nucleotides proximal to the RNase P site and it explains why in the absence of RNase III the 1st tRNA in the T4 tRNA cluster, tRNAGln, does not accumulate.This publication has 22 references indexed in Scilit:
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