An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase

Zhihua Zhou, Murray P Deutscher

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

Escherichia coli cells lacking both polynucleotide phosphorylase (PNPase) and RNase PH, the only known P1-dependent exoribonucleases, were previously shown to grow slowly at 37°C and to display a dramatically reduced level of tRNA(Tryrsu3+) suppressor activity. Here we show that the RNase PH-negative, PNP-negative double-mutant strain actually displays a reversible cold-sensitive phenotype and that tRNA biosynthesis is normal. In contrast, ribosome structure and function are severely affected, particularly at lower temperatures. At 31°C, the amount of 50S subunit is dramatically reduced and 23S rRNA is degraded. Moreover, cells that had been incubated at 42°C immediately cease growing and synthesizing protein upon a shift to 31°C, suggesting that the ribosomes synthesized at the higher temperature are defective and unable to function at the lower temperature. These data indicate that RNase PH and PNPase play an essential role that affects ribosome metabolism and that this function cannot be taken over by any of the hydrolytic exoribonucleases present in the cell.

Original languageEnglish
Pages (from-to)4391-4395
Number of pages5
JournalJournal of Bacteriology
Volume179
Issue number13
StatePublished - Jul 1 1997

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Exoribonucleases
Polyribonucleotide Nucleotidyltransferase
Ribosomes
Phosphates
Transfer RNA
Temperature
Escherichia coli
Phenotype
ribonuclease PH
Proteins

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase. / Zhou, Zhihua; Deutscher, Murray P.

In: Journal of Bacteriology, Vol. 179, No. 13, 01.07.1997, p. 4391-4395.

Research output: Contribution to journalArticle

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