A dual role for the <i>Bacillus subtilis glpD</i> leader and the GlpP protein in the regulated expression of <i>glpD</i>: antitermination and control of mRNA stability

Glatz, Elisabeth; Nilsson, Rune‐Pär; Rutberg, Lars; Rutberg, Blanka

doi:10.1046/j.1365-2958.1996.376903.x

Cited by 54 publications

(48 citation statements)

References 27 publications

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“…This is a known mechanism for stabilizing or destabilizing transcripts. For example, B. subtilis glpD mRNA can be stabilized by the GlpP antiterminator protein (Glatz et al, 1996) and in E. coli, the ompA and glgC transcripts are destabilized by the Hfq and CsrA proteins, respectively (Vytvytska et al, 1998, Liu & Romeo, 1997. Finally, we wish to point out that there are striking sequence similarities between the sequence around the aprE RBS and that of a polypurine-rich sequence in bacteriophage SP82 which functions as a 5h stabilizer in B. subtilis (Hue et al, 1995).…”

Section: Discussionmentioning

confidence: 98%

The aprE leader is a determinant of extreme mRNA stability in Bacillus subtilis

2000

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The Bacillus subtilis aprE gene encodes subtilisin, an extracellular proteolytic enzyme produced in stationary phase. The authors examined the stability of aprE mRNA and aprE leader-lacZ fusion mRNA. Both mRNAs were found to be unusually stable, with half-lives longer than 25 min, demonstrating that the aprE leader contains a determinant for extreme mRNA stability. The half-lives were the same in growing and stationary-phase cells. This contrasts with the findings of O. Resnekov et al. (1990) [Proc Natl Acad Sci U S A 87, 8355-8359], which suggested a growth-phase-dependent mechanism for decay of aprE mRNA. The discrepancy is explained by the techniques used. Substitution of two bases or deletion of 25 nucleotides in the aprE leader led to a major difference in its predicted secondary structure and resulted in a fivefold reduction of the half-life of aprE mRNA. The authors also determined the halflife of amyE mRNA, which encodes α-amylase, another stationary-phase, excreted enzyme and found it to be around 5 min. This shows that extreme stability is not a general property of stationary-phase mRNAs encoding excreted enzymes.

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Section: Discussionmentioning

confidence: 98%

The aprE leader is a determinant of extreme mRNA stability in Bacillus subtilis

2000

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“…Among the B. subtilis mRNAs targeted by the RppH-dependent pathway is the 2.2-kb transcript of the yhxA-glpP operon, which encodes a transcription antiterminator (GlpP) important for regulating the synthesis of glycerol-3-phosphate dehydrogenase (11). The lifetime of this transcript can be prolonged in B. subtilis by deleting the rppH gene, by depleting the 5′-exonuclease subunit of RNase J, or by adding a 5′-terminal stem loop, an RNA modification that prevents 5′ attack by both RppH (7) and RNase J (4).…”

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confidence: 99%

Specificity of RppH-dependent RNA degradation in Bacillus subtilis

Hsieh

Richards

Liu

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Bacterial RNA degradation often begins with conversion of the 5′-terminal triphosphate to a monophosphate, creating a better substrate for subsequent ribonuclease digestion. For example, in Bacillus subtilis and related organisms, removal of the gamma and beta phosphates of primary transcripts by the RNA pyrophosphohydrolase RppH triggers rapid 5′-exonucleolytic degradation by RNase J. However, the basis for the selective targeting of a subset of cellular RNAs by this pathway has remained largely unknown. Here we report that purified B. subtilis RppH requires at least two unpaired nucleotides at the 5′ end of its RNA substrates and prefers three or more. The second of these 5′-terminal nucleotides must be G, whereas a less strict preference for a purine is evident at the third position, and A is slightly favored over G at the first position. The same sequence requirements are observed for RppH-dependent mRNA degradation in B. subtilis cells. By contrast, a parallel pathway for 5′-end-dependent RNA degradation in that species appears to involve an alternative phosphate-removing enzyme that is relatively insensitive to sequence variation at the first three positions.O f the mechanisms that control gene expression in all living organisms, mRNA degradation is among the least well understood. Within the same cell, the half-lives of distinct mRNAs can differ by up to two orders of magnitude (seconds to an hour in bacteria, minutes to more than a day in higher eukaryotes), with proportionate effects on mRNA levels (1). In addition, the lifetimes of many messages can be modulated in response to environmental signals.Although it was originally assumed that Escherichia coli could serve as a paradigm for mRNA degradation in all bacteria, it is now clear that many bacterial species use a different set of ribonucleases and distinct mechanisms to degrade mRNA. A gamma proteobacterium, E. coli generally relies on the essential endonuclease RNase E to cleave transcripts internally, generating RNA fragments that are then degraded to mononucleotides by a combination of further RNase E cleavage and 3′-exonuclease digestion (1). Remarkably, despite its crucial role in E. coli, RNase E is entirely absent from a large number of other bacteria, including many Gram-positive species and even some Gram-negative proteobacteria (2). Instead, those species generally contain one or more ribonucleases that are absent from E. coli. For example, Bacillus subtilis, Staphylococcus aureus, and Helicobacter pylori contain two such ribonucleases-RNase Y, a membraneassociated endonuclease, and RNase J, a 5′-monophosphatedependent 5′ exonuclease that is also capable of acting as an endonuclease-in addition to a number of 3′ exonucleases (2-6).Because primary transcripts in B. subtilis are protected from exonucleolytic degradation by their 5′-terminal triphosphate and 3′-terminal stem loop, it was initially believed that message degradation in that species bypasses those termini and begins with endonucleolytic cleavage, generating RNA fragments with un...

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“…When the wild-type glpP gene is introduced into these strains the glpD mRNA is stabilized. Introduction of glpP also restores glucose repression indicating that it is mediated by the GlpP protein (Glatz et al, 1996).…”

Section: The Glp Regulon Of B Subtilismentioning

confidence: 94%

“…For the glpD operon it has been shown that full-length transcripts are obtained under inducing conditions, while under non-inducing conditions, the transcripts terminate at nucleotides in the downstream stem of the terminator (Holmberg and Rutberg, 1991;. Point mutations and deletions within the glpD terminator sequence lead to constitutive, GlpP-and G3P-independent expression of glpD (Glatz et al, 1996). They also result in glucose-repression-insensitive expression of glpD.…”

Section: The Glp Regulon Of B Subtilismentioning

confidence: 99%

Antitermination of transcription of catabolic operons

Rutberg¹

1997

Molecular Microbiology

103

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SummaryAntitermination of transcription mediated by proteins interacting with mRNA sequences is described for nine operons/regulons. Eight of the systems are catabolic, while the ninth, the Klebsiella pneumoniae nas regulon, is involved in the assimilation of nitrate and nitrite. Six of the catabolic operons/regulons are found in Bacillus subtilis, one is found in Escherichia coli, and one in Pseudomonas aeruginosa. The antitermination system of five of the operons/regulons (E. coli blg, and sacPA, sacB, bgl, and lic from B. subtilis) are assigned to the bgl-sac family on the basis of extensive similarities with regard to antiterminator proteins and the sequences of the antiterminators. Other members of the bgl-sac family are the arb operon of Erwinia chrysanthemi and a presumed bgl operon of Lactococcus lactis. The antitermination systems of the other four operons/regulons (B. subtilis glp, B. subtilis hut, P. aeruginosa ami, and K. pneumoniae nas) seem to be unrelated both to the bgl-sac family and to each other. The antiterminator protein of the B. subtilis glp regulon has been found not only to cause antitermination but also to stabilize the resultant mRNA and to mediate glucose repression. If other antiterminator proteins, and antitermination factors, also prove to have additional functions, it will broaden the impact of antitermination as a means of controlling gene expression.

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A dual role for the Bacillus subtilis glpD leader and the GlpP protein in the regulated expression of glpD: antitermination and control of mRNA stability

Cited by 54 publications

References 27 publications

The aprE leader is a determinant of extreme mRNA stability in Bacillus subtilis

The aprE leader is a determinant of extreme mRNA stability in Bacillus subtilis

Specificity of RppH-dependent RNA degradation in Bacillus subtilis

Antitermination of transcription of catabolic operons

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