PMID:23241393

Citation	Mohanty, BK and Kushner, SR (2013) Deregulation of poly(A) polymerase I in Escherichia coli inhibits protein synthesis and leads to cell death. Nucleic Acids Res. 41:1757-66
Abstract	Polyadenylation plays important roles in RNA metabolism in both prokaryotes and eukaryotes. Surprisingly, deregulation of polyadenylation by poly(A) polymerase I (PAP I) in Escherichia coli leads to toxicity and cell death. We show here that mature tRNAs, which are normally not substrates for PAP I in wild-type cells, are rapidly polyadenylated as PAP I levels increase, leading to dramatic reductions in the fraction of aminoacylated tRNAs, cessation of protein synthesis and cell death. The toxicity associated with PAP I is exacerbated by the absence of either RNase T and/or RNase PH, the two major 3' → 5' exonucleases involved in the final step of tRNA 3'-end maturation, confirming their role in the regulation of tRNA polyadenylation. Furthermore, our data demonstrate that regulation of PAP I is critical not for preventing the decay of mRNAs, but rather for maintaining normal levels of functional tRNAs and protein synthesis in E. coli, a function for polyadenylation that has not been observed previously in any organism.
Links	PubMed PMC3561954 Online version:10.1093/nar/gks1280
Keywords	Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/metabolism; Exoribonucleases/genetics; Exoribonucleases/metabolism; Mutation; Phenotype; Polyadenylation; Polynucleotide Adenylyltransferase/metabolism; Protein Biosynthesis; RNA, Transfer/metabolism
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