Regulation of RraA, a Protein Inhibitor of RNase E-Mediated RNA Decay

Zhao, Meng; Zhou, Li; Kawarasaki, Yasuaki; Georgiou, George

doi:10.1128/jb.188.9.3257-3263.2006

Cited by 23 publications

(22 citation statements)

References 37 publications

(41 reference statements)

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“…Together, these results imply that at least this SPT is degraded by a different pathway from other GAS mRNAs and that PNPase is rate limiting for its decay. We expect, therefore, that in stationary phase, SPTs become stable because they are either protected from this specific decay pathway (27,38) or because this pathway becomes defective or inactive in stationary phase.…”

Section: Discussionmentioning

confidence: 99%

Role of mRNA Stability in Growth Phase Regulation of Gene Expression in the Group A Streptococcus

2007

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The impressive disease spectrum of Streptococcus pyogenes (the group A streptococcus [GAS]) is believed to be determined by its ability to modify gene expression in response to environmental stimuli. Virulence gene expression is controlled tightly by several different transcriptional regulators in this organism. In addition, expression of most, if not all, GAS genes is determined by a global mechanism dependent on growth phase. To begin an analysis of growth-phase regulation, we compared the transcriptome 2 h into stationary phase to that in late exponential phase of a serotype M3 GAS strain. We identified the arc transcript as more abundant in stationary phase in addition to the sag and sda transcripts that had been previously identified. We found that in stationary phase, the stability of sagA, sda, and arcT transcripts increased dramatically. We found that polynucleotide phosphorylase (PNPase [encoded by pnpA]) is rate limiting for decay of sagA and sda transcripts in late exponential phase, since the stability of these mRNAs was greater in a pnpA mutant, while stability of control mRNAs was unaffected by this mutation. Complementation restored the wild-type decay rate. Furthermore, in a pnpA mutant, the sagA mRNA appeared to be full length, as determined by Northern hybridization. It seems likely that mRNAs abundant in stationary phase are insensitive to the normal decay enzyme(s) and instead require PNPase for this process. It is possible that PNPase activity is limited in stationary phase, allowing persistence of these important virulence factor transcripts at this phase of growth.

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Section: Discussionmentioning

confidence: 99%

Role of mRNA Stability in Growth Phase Regulation of Gene Expression in the Group A Streptococcus

2007

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“…The expression of the rraA gene was previously shown to be induced in stationary phase (56). Northern blot analysis (see Fig.…”

Section: Resultsmentioning

confidence: 99%

“…3C). Finally, the glmS852:: Tn5 allele did not affect the LacZ activity from a chromosomal ⌽(PrraA-lacZ) fusion (56), indicating that the impairment of glmS specifically enhances the transcription of rraB but not that of the other RNase E inhibitor, rraA (data not shown).…”

Section: Vol 191 2009 Transcriptional Regulation Of E Coli Rrab 6669mentioning

confidence: 99%

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confidence: 99%

“…Third, the membrane localization of RNase E and its association with the bacterial cytoskeleton may affect its function through various mechanisms (25,31,51). Finally, our lab has shown that the activity of RNase E is affected globally by the endoribonuclease binding proteins RraA and RraB, which control the decay and abundance of large numbers of bacterial mRNAs in trans (16,29,54,56).RraB, previously annotated as YjgD in the NCBI database, is a 15.6-kDa protein that interacts with RNase E and inhibits RNase E endonucleolytic cleavages in E. coli. In contrast to RraA homologues, which exist in numerous bacterial genomes, RraB is found only in gammaproteobacteria, suggesting that the latter protein may have a more specialized role in modulating RNA degradation.…”

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Transcriptional Regulation of theEscherichia coliGenerraB, Encoding a Protein Inhibitor of RNase E

et al. 2009

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The Escherichia coli RNA degradosome is a protein complex that plays a critical role in the turnover of numerous RNAs. The key component of the degradosome complex is the endoribonuclease RNase E, a multidomain protein composed of an N-terminal catalytic region and a C-terminal region that organizes the other protein components of the degradosome. Previously, the RNase E inhibitors RraA and RraB were identified genetically and shown to bind to the C-terminal region of RNase E, thus affecting both the protein composition of the degradosome and the endonucleolytic activity of RNase E. In the present work, we investigated the transcriptional regulation of rraB. rraB was shown to be transcribed constitutively from its own promoter, PrraB. Transposon mutagenesis and screening for increased ␤-galactosidase activity from a chromosomal PrraB-lacZ transcriptional fusion resulted in the isolation of a transposon insertion in glmS, encoding the essential enzyme glucosamine-6-phosphate synthase that catalyzes the first committed step of the uridine 5-diphospho-N-acetyl-glucosamine (UDP-GlcNAc) pathway, which provides intermediates for peptidoglycan biogenesis. The glmS852::Tn5 allele resulted in an approximately 50% lower intracellular concentration of UDP-GlcNAc and conferred a fivefold increase in the level of rraB mRNA. This allele also mediated a twofold increase in ␤-galactosidase activity from a chromosomal fusion of the 5 untranslated region of the rne gene to lacZ, suggesting that a reduction in cellular concentration of UDP-GlcNAc and the resulting increased expression of RraB might modulate the action of RNase E.The endoribonuclease RNase E plays a central role in RNA metabolism, including the processing of rRNAs and tRNAs (30,42,43); the degradation of small regulatory RNAs; and, most importantly, the turnover of numerous cellular mRNAs in Escherichia coli (5,13,23,33). Homologous RNase E has been identified in more than 50 bacteria, archaea, and plants (28). The 1,061-amino-acid E. coli RNase E protein can be divided into functional portions, from the N terminus to the C terminus, as follows. The N-terminal half (amino acid residues 1 to 529) contains the endonuclease active site (amino acid residues 1 to 395) and a zinc finger region (amino acid residues 400 to 415) (8, 9). The central region includes the membrane anchoring segment A (amino acid residues 565 to 582) and its flanking portions (25) as well as an arginine-rich RNA binding site (amino acid residues 604 to 688) (34). The C-terminal half (amino acid residues 734 to 1061) is an unstructured scaffold domain that contains binding sites for the other core degradosome components, namely, polynucleotide phosphorylase, the RhlB helicase, and the glycolytic enzyme enolase (11,35,45,46,53). Previous studies indicate that the assembled degradosome complex is necessary for normal mRNA degradation and the degradosome components functionally interact during decay of at least some RNAs in E. coli (4,24).The cellular level and activity of RNase E in E. coli are und...

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Enolase binds to RnpA in competition with PNPase in Staphylococcus aureus

Wang

Chen

et al. 2017

FEBS Letters

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The RNA degradosome of the pathogen Staphylococcus aureus regulates the metabolism of RNA, the expression of virulence factors, and the formation of biofilms. It is composed of the RNases J1/J2, RNase Y, CshA, PNPase, Enolase, Pfk, and a newly identified component, RnpA. However, the function and new partners of RnpA in RNA degradosome remain unknown. Here, we identified PNPase and Enolase as two novel partners for RnpA. Further studies revealed that Enolase interacts with RnpA in competition with PNPase. Enzymatic assays showed that RnpA increases Enolase activity but has no effect on PNPase. These findings provide more information about the functional relationship between RnpA and RNA degradosome.

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Regulation of RraA, a Protein Inhibitor of RNase E-Mediated RNA Decay

Cited by 23 publications

References 37 publications

Role of mRNA Stability in Growth Phase Regulation of Gene Expression in the Group A Streptococcus

Role of mRNA Stability in Growth Phase Regulation of Gene Expression in the Group A Streptococcus

Transcriptional Regulation of theEscherichia coliGenerraB, Encoding a Protein Inhibitor of RNase E

Enolase binds to RnpA in competition with PNPase in Staphylococcus aureus

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