The Decay of Bacterial Messenger RNA

Nierlich, Donald P.; Murakawa, George J.

doi:10.1016/s0079-6603(08)60967-8

Cited by 83 publications

(59 citation statements)

References 250 publications

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“…Based on these results, it has been suggested that one of the functions of the stem-loop structure located at the 3′-end of most chloroplast genes is to prevent polyadenylation, which is followed by degradation (12). Most of the E.coli mRNAs are also characterized by a stem-loop structure at the 3′-end (9). In order to determine whether PAP I activity is modulated by the structure of the RNA, RNA molecules in which the stem-loop structure was located either at the 3′-end or in the middle of the molecule were tested in an in vitro polyadenylation assay.…”

Section: Binding Affinities Of Pap I To Ribohomopolymersmentioning

confidence: 99%

“…These results suggested that in contrast to the nucleus and cytoplasm of eukaryotic cells, where the poly(A) tail is important for stability, maturation and translation of mRNA, the addition of poly(A) tails in bacterial mRNAs promotes their degradation. Taken together, polyadenylation of RNA molecules is part of the molecular mechanism of RNA degradation in bacteria (1,2,(9)(10)(11). Similarly to bacterial cells, polyadenylation of RNA molecules during the degradation process has been described in chloroplasts and in mitochondria, cellular organelles that are believed to have arisen in an evolutionary manner from a prokaryotic ancestor (12)(13)(14)(15).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the E.coli poly(A) polymerase: nucleotide specificity, RNA-binding affinities and RNA structure dependence

Yehudai‐Resheff

Schuster

2000

Nucleic Acids Research

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Polyadenylation of RNA molecules in bacteria and chloroplasts has been implicated as part of the RNA degradation pathway. The polyadenylation reaction is performed in Escherichia coli mainly by the enzyme poly(A) polymerase I (PAP I). In order to understand the molecular mechanism of RNA polyadenylation in bacteria, we characterized the biochemical properties of this reaction in vitro using the purified enzyme. Unlike the PAP from yeast nucleus, which is specific for ATP, E.coli PAP I can use all four nucleotide triphosphates as substrates for addition of long ribohomopolymers to RNA. PAP I displays a high binding activity to poly(U), poly(C) and poly(A) ribohomopolymers, but not to poly(G). The 3′-ends of most of the mRNA molecules in bacteria are characterized by a stem-loop structure. We show here that in vitro PAP I activity is inhibited by a stem-loop structure. A tail of two to six nucleotides located 3′ to the stem-loop structure is sufficient to overcome this inhibition. These results suggest that the stem-loop structure located in most of the mRNA 3′-ends may function as an inhibitor of polyadenylation and degradation of the corresponding RNA molecule. However, RNA 3′-ends produced by endonucleolytic cleavage by RNase E in single-strand regions of mRNA molecules may serve as efficient substrates for polyadenylation that direct these molecules for rapid exonucleolytic degradation.

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Section: Binding Affinities Of Pap I To Ribohomopolymersmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of the E.coli poly(A) polymerase: nucleotide specificity, RNA-binding affinities and RNA structure dependence

Yehudai‐Resheff

Schuster

2000

Nucleic Acids Research

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“…In silico studies revealed that 5h-UTR can form several alternative secondary structures with few unpaired nucleotides and energy levels as high as 29n5 kcal mol −" (123 kJ mol −" ) (results not shown). 5h-UTR sequences were detected in several mRNAs from different bacteria like E. coli, Rhodobacter capsulatus and B. subtilis (for reviews see Nierlich & Murakawa, 1996 ;Kushner, 1996 ;Coburn & Mackie, 1999), and mRNAs from coldshock genes from Lc. lactis (Wouters et al, 1998) and E. coli (Jiang et al, 1996 ;Fang et al, 1998).…”

Section: Characterization Of Pmanmentioning

confidence: 99%

The gene encoding IIABL Man in Streptococcus salivarius is part of a tetracistronic operon encoding a phosphoenolpyruvate:mannose/glucose phosphotransferase system The GenBank accession number for the sequence reported in this paper is AF130465.

et al. 2000

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Glucose and mannose are transported in streptococci by the mannose-PTS (phosphoenolpyruvate :mannose phosphotransferase system), which consists of a cytoplasmic IIAB protein, called IIAB Man , and an uncharacterized membrane permease. This paper reports the characterization of the man operon encoding the specific components of the mannose-PTS of Streptococcus salivarius. The man operon was composed of four genes, manL, manM , manN and manO. These genes were transcribed from a canonical promoter (Pman) into a 36 kb polycistronic mRNA that contained a 5'-UTR (untranslated region). The predicted manL gene product encoded a 355 kDa protein and contained the amino acid sequences of the IIA and IIB phosphorylation sites already determined from purified S. salivarius IIAB

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“…Messages often decay more rapidly when rendered devoid of ribosomes by introduction of a stop codon or by the action of certain antibiotics that impair ribosome function (see Nierlich and Murakawa, 1996; and references therein). On the other hand, in the presence of antibiotics that are thought to 'freeze' ribosomes on the message, the RNA is stabilized.…”

Section: Introductionmentioning

confidence: 99%

Escherichia coli RNase III (rnc) autoregulation occurs independently of rnc gene translation

Matsunaga

Simons

1997

Molecular Microbiology

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SummaryControl of mRNA stability is an established means of regulating gene expression. However, the detailed mechanisms by which such control is achieved are only now emerging. In particular, there remains a question about the involvement of translation. Escherichia coli ribonuclease III (RNase III) negatively autoregulates expression of its own gene (rnc) approximately 10-fold, by cleaving the untranslated leader and initiating approximately 10-fold more rapid decay of the rnc mRNA, after which RNase III plays no further role. Here, we define the mechanism of this control further. Mutations that increase rnc gene translation abolish autoregulation by increasing the stability of the RNase III-cleaved transcript RNA approximately 10-fold, with no effect on the uncleaved species. Mutations that decrease translation destabilize the rnc mRNA in the presence or absence of RNase III. In so doing, they reveal a pathway of rnc transcript decay distinct from the RNase III-dependent pathway. Stability of a 'minirnc' transcript containing the rnc leader and only the first two codons of the rnc gene is unaffected by decreased translation, presumably because sequences required for this pathway were removed. Importantly, this mini-rnc transcript is regulated normally by RNase III. Moreover, rnc transcripts synthesized in vitro do not decay in cell-free extracts lacking ribosomes, unless they are first cleaved by RNase III. These two results show that RNase III cleavage can initiate rnc transcript decay independently of rnc gene translation, unambiguously establishing that control of mRNA decay need not involve changes in translation. How rnc gene translation is optimized for efficient autoregulation will also be discussed.

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The Decay of Bacterial Messenger RNA

Cited by 83 publications

References 250 publications

Characterization of the E.coli poly(A) polymerase: nucleotide specificity, RNA-binding affinities and RNA structure dependence

Characterization of the E.coli poly(A) polymerase: nucleotide specificity, RNA-binding affinities and RNA structure dependence

The gene encoding IIABL Man in Streptococcus salivarius is part of a tetracistronic operon encoding a phosphoenolpyruvate:mannose/glucose phosphotransferase system The GenBank accession number for the sequence reported in this paper is AF130465.

Escherichia coli RNase III (rnc) autoregulation occurs independently of rnc gene translation

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