2015
DOI: 10.1093/nar/gkv1302
|View full text |Cite
|
Sign up to set email alerts
|

Ribonucleoprotein particles of bacterial small non-coding RNA IsrA (IS61 or McaS) and its interaction with RNA polymerase core may link transcription to mRNA fate

Abstract: Coupled transcription and translation in bacteria are tightly regulated. Some small RNAs (sRNAs) control aspects of this coupling by modifying ribosome access or inducing degradation of the message. Here, we show that sRNA IsrA (IS61 or McaS) specifically associates with core enzyme of RNAP in vivo and in vitro, independently of σ factor and away from the main nucleic-acids-binding channel of RNAP. We also show that, in the cells, IsrA exists as ribonucleoprotein particles (sRNPs), which involve a defined set … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1

Citation Types

0
17
0

Year Published

2017
2017
2020
2020

Publication Types

Select...
7
2

Relationship

0
9

Authors

Journals

citations
Cited by 19 publications
(17 citation statements)
references
References 64 publications
0
17
0
Order By: Relevance
“…One possibility is that ProQ becomes recruited into multicomponent assemblies for which the interactions and specificities may be distributed among the components. The reported association of ProQ with the ribosome (Sheidy and Zielke 2013) and its presence in a super-complex including RNA polymerase, PNPase, and RNA (van Nues et al 2016) could help to steer the preferred in vivo binding sites for ProQ. On the other hand, ProQ might also compete for binding sites with other proteins and chaperones, with important functional consequence.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…One possibility is that ProQ becomes recruited into multicomponent assemblies for which the interactions and specificities may be distributed among the components. The reported association of ProQ with the ribosome (Sheidy and Zielke 2013) and its presence in a super-complex including RNA polymerase, PNPase, and RNA (van Nues et al 2016) could help to steer the preferred in vivo binding sites for ProQ. On the other hand, ProQ might also compete for binding sites with other proteins and chaperones, with important functional consequence.…”
Section: Discussionmentioning
confidence: 99%
“…The previously reported association with such diverse systems as the ribosome (Sheidy and Zielke 2013) and a super-complex including RNA polymerase, PNPase, and RNA (van Nues et al 2016) raise tantalizing possibilities for the biological function of ProQ. Might ProQ be involved in modulating the process of translation by affecting secondary structure features of its targets?…”
Section: Discussionmentioning
confidence: 99%
“…Like Hfq proteins, FinO-domain proteins may be involved in modulating RNA degradation or ribosome binding, which occurs after the annealing between the sRNA and mRNA. In line with this, it was found that the overexpression of FinP leads to the degradation of traJ mRNA (Lee et al, 1992), and overexpression of RocR sRNA decreases comEA mRNA levels (Attaiech et al, 2016) Additionally, E. coli ProQ was proposed to interact with ribonucleoprotein complexes involved in RNA metabolism (van Nues et al, 2016) and was found to be associated with ribosomes, in a manner that was dependent on the presence of mRNAs (Sheidy and Zielke, 2013). Clearly, the consequences of FinOdomain protein binding to RNAs are an area ripe for further investigation.…”
Section: Fino-domain Protein Binding To Rna May Have Multiple Consequmentioning
confidence: 95%
“…McaS is a multi-cellular adhesive small regulatory RNA and is known to regulate flagellar motility and biofilm formation by targeting the global transcription regulators (csgD, flhD) and biofilm formation related mRNA pgaA [27, 36]. Protein co-purification study also found that McaS could bind with RpsA (translation initiation factor), Lon (DNA-binding ATP-dependent protease), PNPase (polynucleotide phosphorylase or - polymerase), AtpA (F1 sector of membrane-bound ATP synthase), CsrA (Regulatory McaS protein for carbon source metabolism) [37]. The targets of McaS match well to the known persister pathways including global regulator, biofilm formation, trans-translation, protease and energy production [7], which can count for the role of McaS in persistence.…”
Section: Discussionmentioning
confidence: 99%