<i>N. meningitidis</i>1681 is a member of the FinO family of RNA chaperones

Chaulk, Steven G.; Lu, Ji; Tan, Kun; Dc, Arthur; Ra, Edwards; Ls, Frost; Joachimiak, A.; Jn, Glover

doi:10.4161/rna.7.6.13688

Cited by 31 publications

(63 citation statements)

References 36 publications

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“…The contribution of RNA chaperones to RNA pairing can involve acceleration of their annealing or the stabilization of the final complex formed by paired RNAs. The F plasmid FinO, E. coli ProQ and N. meningitidis NMB1681 proteins increased the rates of RNA annealing and strand exchange in in vitro assays using FinP sRNA and traJ mRNA fragments (van Biesen and Frost, ; Arthur et al ., ; Chaulk et al ., ). This role is reminiscent of the Hfq protein (Soper et al ., ; Wroblewska and Olejniczak, ).…”

Section: Outcomes Of Fino‐domain Protein Binding To Rnamentioning

confidence: 97%

“…However, unlike FinO domain mutations, the C‐terminal truncations did not affect RocR sRNA lifetime, indicating that while the FinO domain is sufficient for sRNA binding, both the FinO and C‐terminal domains participate in repression of the target mRNA (Attaiech et al ., ). On the other hand, N. meningitidis NMB1681, which consists only of a FinO domain, was still capable of promoting RNA duplex formation (Chaulk et al ., ). Overall, these observations are consistent with a model in which the FinO domain is critical for RNA binding but the extensions contribute other functions related to the regulation.…”

Section: Outcomes Of Fino‐domain Protein Binding To Rnamentioning

confidence: 97%

“…). As a consequence, initially all in vitro studies of FinO, ProQ and Neisseria NMB1681 binding to RNA were carried out with this single RNA pair (Jerome and Frost, ; Ghetu et al ., ; Chaulk et al ., ; Arthur et al ., ).…”

Section: Rnas Bound By Fino‐domain Proteinsmentioning

confidence: 99%

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ProQ/FinO‐domain proteins: another ubiquitous family of RNA matchmakers?

Olejniczak

Storz

2017

Molecular Microbiology

131

124

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Summary Small RNAs (sRNAs), particularly those that act by limited base pairing with mRNAs, are part of most regulatory networks in bacteria. In many cases, the base-pairing interaction is facilitated by the RNA chaperone Hfq. However, not all bacteria encode Hfq and some base-pairing sRNAs do not require Hfq raising the possibility of other RNA chaperones. Candidates are proteins with homology to FinO, a factor that promotes base pairing between the FinP antisense sRNA and the traJ mRNA to control F plasmid transfer. Recent papers have shown that the Salmonella enterica FinO-domain protein ProQ binds a large suite of sRNAs, including the RaiZ sRNA, which represses translation of the hupA mRNA, and the Legionella pneumophila protein RocC binds the RocR sRNA, which blocks expression of competence genes. Here we discuss what is known about FinO-domain structures, including the recently solved Escherichia coli ProQ structure, as well as the RNA binding properties of this family of proteins and evidence they act as chaperones. We compare these properties with those of Hfq. We further summarize what is known about the physiological roles of FinO-domain proteins and enumerate outstanding questions whose answers will establish whether they constitute a second major class of RNA chaperones.

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Section: Outcomes Of Fino‐domain Protein Binding To Rnamentioning

confidence: 97%

Section: Outcomes Of Fino‐domain Protein Binding To Rnamentioning

confidence: 97%

See 1 more Smart Citation

ProQ/FinO‐domain proteins: another ubiquitous family of RNA matchmakers?

Olejniczak

Storz

2017

Molecular Microbiology

131

124

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“…4D). This is a routine test in RNA chaperone studies (for example, Chaulk et al 2011). The exchange thus initiated resulted in progressive liberation of labeled 5S rRNA, and its mobility in native gel was slower than that of 5S rRNA Mg .…”

Section: Premrp-l18 and Rhodanese Form The Minimal 5s Rrna Mitochondrmentioning

confidence: 99%

Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18

Smirnov

Entelis²,

Martin³

et al. 2011

Genes Dev.

107

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5S rRNA is an essential component of ribosomes of all living organisms, the only known exceptions being mitochondrial ribosomes of fungi, animals, and some protists. An intriguing situation distinguishes mammalian cells: Although the mitochondrial genome contains no 5S rRNA genes, abundant import of the nuclear DNA-encoded 5S rRNA into mitochondria was reported. Neither the detailed mechanism of this pathway nor its rationale was clarified to date. In this study, we describe an elegant molecular conveyor composed of a previously identified human 5S rRNA import factor, rhodanese, and mitochondrial ribosomal protein L18, thanks to which 5S rRNA molecules can be specifically withdrawn from the cytosolic pool and redirected to mitochondria, bypassing the classic nucleolar reimport pathway. Inside mitochondria, the cytosolic 5S rRNA is shown to be associated with mitochondrial ribosomes.

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“…2D). NMB1681 also has significant RNA binding, strand‐exchange and duplexing activities in vitro (Chaulk et al ., 2010). Remarkably, NMB1681 is able to partially restore conjugative repression to finO ‐deficient E. coli in vivo even though its ability to protect FinP from degradation is relatively weak (Chaulk et al ., 2010).…”

Section: Post‐transcriptional Regulation Of Trajmentioning

confidence: 99%

Relaxosome function and conjugation regulation in F‐like plasmids – a structural biology perspective

Wong

Glover

2012

Molecular Microbiology

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Summary The tra operon of the prototypical F plasmid and its relatives enables transfer of a copy of the plasmid to other bacterial cells via the process of conjugation. Tra proteins assemble to form the transferosome, the transmembrane pore through which the DNA is transferred, and the relaxosome, a complex of DNA‐binding proteins at the origin of DNA transfer. F‐like plasmid conjugation is characterized by a high degree of plasmid specificity in the interactions of tra components, and is tightly regulated at the transcriptional, translational and post‐translational levels. Over the past decade, X‐ray crystallography of conjugative components has yielded insights into both specificity and regulatory mechanisms. Conjugation is repressed by FinO, an RNA chaperone which increases the lifetime of the small RNA, FinP. Recent work has resulted in a detailed model of FinO/FinP interactions and the discovery of a family of FinO‐like RNA chaperones. Relaxosome components include TraI, a relaxase/helicase, and TraM, which mediates signalling between the transferosome and relaxosome for transfer initiation. The structures of TraI and TraM bound to oriT DNA reveal the basis of specific recognition of DNA for their cognate plasmid. Specificity also exists in TraI and TraM interactions with the transferosome protein TraD.

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N. meningitidis1681 is a member of the FinO family of RNA chaperones

Cited by 31 publications

References 36 publications

ProQ/FinO‐domain proteins: another ubiquitous family of RNA matchmakers?

ProQ/FinO‐domain proteins: another ubiquitous family of RNA matchmakers?

Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18

Relaxosome function and conjugation regulation in F‐like plasmids – a structural biology perspective

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