RNA processing by RNase III is involved in the synthesis of Escherichia coli polynucleotide phosphorylase.
The synthesis of Escherichia coli polynucleotide phosphorylase (PNPase) was examined in a mutant strain defective in the RNA processing enzyme RNase III (Rnc-). We found that the specific activity and the synthesis rate of PNPase were increased in the Rnc- strain by more than three times that in an Rnc+ strain. Such increased synthesis of PNPase was not observed in a mutant strain transformed with a plasmid carrying the rnc+ gene. Quantitative analysis of RNA showed that the transcripts from the pnp gene, which encodes PNPase, were degraded more slowly in the Rnc- strain than in the Rnc+ strain. These results indicate that processing of the transcripts by RNase III is intimately involved in controlling the expression of pnp by affecting the stability of its messenger RNA.
Takata
R
R
Department of Biology, Saga Medical School, Japan.
Mukai
T
T
Hori
K
K
D004262:DNA Restriction Enzymes; D004722:Endoribonucleases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D005796:Genes; D005798:Genes, Bacterial; D009154:Mutation; D009876:Operon; D011117:Polyribonucleotide Nucleotidyltransferase / Q000096:biosynthesis / Q000235:genetics*; D012323:RNA Processing, Post-Transcriptional; D043244:Ribonuclease III; D014158:Transcription, Genetic
D029968:Escherichia coli Proteins; D011117:Polyribonucleotide Nucleotidyltransferase; D004722:Endoribonucleases; D004262:DNA Restriction Enzymes; D043244:Ribonuclease III; C468366:ribonuclease III, E coli