Potential Regulatory Interactions of Escherichia coli RraA Protein with DEAD-box Helicases

Pietras, Zbigniew; Hardwick, Steven W.; Świeżewski, Szymon; Luisi, Ben F.

doi:10.1074/jbc.m113.502146

Cited by 12 publications

(9 citation statements)

References 49 publications

(67 reference statements)

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“…How the helicase itself would be regulated is not known, but in E. coli, regulatory proteins that inhibit the RhlB helicase have been described. 8,9 Another more direct explanation for the requirement of a DEAD-box RNA helicase in turnover would be the presence of secondary structures that perform a biological function, such as regulating the accessibility of the ribosomebinding site. For the degradation of such RNAs, the degradosome needs to be assisted by a helicase since it was shown Table 2.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to these 2 domains, composing the core of DEAD box helicases, they can possess N-or C-terminal extensions that can drive specific interactions with RNA 7 or regulatory proteins. 8,9 DEAD box RNA helicases function by coupling ATP binding and hydrolysis to changes in affinity for RNA. Many DEAD-box proteins use this basic mechanism for a mode of RNA helicase activity, separating the strands of short RNA duplexes in a process that involves no translocation.…”

Section: Introductionmentioning

confidence: 99%

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The C-terminal region of the RNA helicase CshA is required for the interaction with the degradosome and turnover of bulk RNA in the opportunistic pathogenStaphylococcus aureus

et al. 2015

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Staphylococcus aureus is a versatile opportunistic pathogen that adapts readily to a variety of different growth conditions. This adaptation requires a rapid regulation of gene expression including the control of mRNA abundance. The CshA DEAD-box RNA helicase was previously shown to be required for efficient turnover of the agr quorum sensing mRNA. Here we show by transcriptome-wide RNA sequencing and microarray analyses that CshA is required for the degradation of bulk mRNA. Moreover a subset of mRNAs is significantly stabilised in absence of CshA. Deletion of the C-terminal extension affects RNA turnover similar to the full deletion of the cshA gene. In accordance with RNA decay data, the C-terminal region of CshA is required for an RNA-independent interaction with components of the RNA degradation machinery. The C-terminal truncation of CshA reduces its ATPase activity and this reduction cannot be compensated at high RNA concentrations. Finally, the deletion of the C-terminal extension does affect growth at low temperatures, but to a significantly lesser degree than the full deletion, indicating that the core of the helicase can assume a partial function and opening the possibility that CshA is involved in different cellular processes.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The C-terminal region of the RNA helicase CshA is required for the interaction with the degradosome and turnover of bulk RNA in the opportunistic pathogenStaphylococcus aureus

et al. 2015

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“…DEAD-box RNA helicases are found in all three domains of life, as well as in some viruses, and they are identified on the basis of highly conserved amino acid motifs within the catalytic core, "D-E-A-D" being one of those motifs (2,3). Besides the conserved catalytic region, they possess variable N-and C-terminal extensions that can regulate the core catalytic activity or coordinate interactions with RNA molecules or proteins (4)(5)(6)(7). The Escherichia coli DbpA RNA helicase, for example, contains an RNA-binding domain (RBD) at the C-terminus, which is responsible for a specific and tight binding to hairpin 92 of 23S ribosomal RNA (8).…”

Section: Introductionmentioning

confidence: 99%

The DEAD-box RNA helicases RhlE2 is a global regulator ofPseudomonas aeruginosalifestyle and pathogenesis

Valentini

Hausmann

González

et al. 2021

Preprint

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The RhlE DEAD-box RNA helicase protein family is widespread among Proteobacteria, but it is the least understood due to the lack of a clear biological function. Here, we study the two RhlE homologs present in the opportunistic pathogen Pseudomonas aeruginosa. RhlE1 and RhlE2 diverged during P. aeruginosa evolution; our data indicate that this resulted in a non-redundant biological role, a distinct molecular action and an enzymatic activity differentially stimulated by RNA. Whereas RhlE1 is specifically necessary for bacteria growth in cold, we show that RhlE2 acts as global post-transcriptional regulator, affecting the level of hundreds of cellular transcripts and multiple functionalities indispensable not only for P. aeruginosa environmental adaptation, but also for its virulence. The global action of RhlE2 relies on a unique C-terminal extension, which establishes an RNA-dependent interaction with the RNase E endonuclease and the cellular RNA degradation machinery.

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“…Pietras et al 20 determined crystal structures of E. coli ribonuclease activity A (RraA) interacting with the DEAD-box RNA helicases RhlB and SrmB. They found that both RhlB and SrmB likely use disordered regions to interact with a common surface on RraA, and that RraA can modulate helicase activity of SrmB, providing a structural model of how RraA-helicase interactions can affect RNA metabolism.…”

Section: Studies On Structural Properties Of Idps and Idprsmentioning

confidence: 99%

Digested disorder, Quarterly intrinsic disorder digest (October-November-December, 2013)

DeForte

Reddy

Uversky

2015

Intrinsically Disordered Proteins

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This is the 4th issue of the Digested Disorder series that represents reader's digest of the scientific literature on intrinsically disordered proteins. The only 2 criteria for inclusion in this digest are the publication date (a paper should be published within the covered time frame) and topic (a paper should be dedicated to any aspect of protein intrinsic disorder). The current digest issue covers papers published during the fourth quarter of 2013; i.e. during the period of October, November, and December of 2013. Similar to previous issues, the papers are grouped hierarchically by topics they cover, and for each of the included paper a short description is given on its major findings.

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Potential Regulatory Interactions of Escherichia coli RraA Protein with DEAD-box Helicases

Cited by 12 publications

References 49 publications

The C-terminal region of the RNA helicase CshA is required for the interaction with the degradosome and turnover of bulk RNA in the opportunistic pathogenStaphylococcus aureus

The C-terminal region of the RNA helicase CshA is required for the interaction with the degradosome and turnover of bulk RNA in the opportunistic pathogenStaphylococcus aureus

The DEAD-box RNA helicases RhlE2 is a global regulator ofPseudomonas aeruginosalifestyle and pathogenesis

Digested disorder, Quarterly intrinsic disorder digest (October-November-December, 2013)

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