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Article

Intragenic suppressors of temperature-sensitive rne mutations lead to the dissociation of RNase E activity on mRNA and tRNA substrates in Escherichia coli.

Nucleic acids research - 1 Sept 2008

Perwez Tariq, Hami Danyal, Maples Valerie F, Min Zhao, Wang Bi-Cheng, Kushner Sidney R

Abstract excerpt

RNase E of Escherichia coli is an essential endoribonuclease that is involved in many aspects of RNA metabolism. Point mutations in the S1 RNA-binding domain of RNase E (rne-1 and rne-3071) lead to temperature-sensitive growth along with defects in 5S rRNA processing, mRNA decay and tRNA maturation. However, it is not clear whether RNase E acts similarly on all kinds of RNA substrates. Here we report the...

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Share to RNA Processing, Post-Transcriptional

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Identifiers

PMID: 18689439
DOI: 10.1093/nar/gkn476
PMCID: PMC2532720

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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