Stem-Loop Structures within mRNA Coding Sequences Activate Translation Initiation and Mediate Control by Small Regulatory RNAs

Initiation is the rate-limiting step of translation, and in bacteria, mRNA secondary structure has been extensively reported as limiting the efficiency of translation by occluding the ribosome-binding site. In striking contrast with this inhibitory effect, we report here that stem-loop structures lo...

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Vydáno v:	Molecular cell Ročník 68; číslo 1; s. 158
Hlavní autoři:	Jagodnik, Jonathan, Chiaruttini, Claude, Guillier, Maude
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 05.10.2017
Témata:	Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Base Pairing Base Sequence Carrier Proteins - genetics Carrier Proteins - metabolism Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Gene Expression Regulation, Bacterial Inverted Repeat Sequences Iron - metabolism Nucleic Acid Conformation Open Reading Frames Peptide Chain Initiation, Translational Receptors, Cell Surface - genetics Receptors, Cell Surface - metabolism Ribosomes - genetics Ribosomes - metabolism RNA, Bacterial - genetics RNA, Bacterial - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism RNA, Small Untranslated - genetics RNA, Small Untranslated - metabolism BAM complex enterobactin Hfq regulatory mechanism non-coding RNA regulatory RNA toeprint translation-activating structure starting block siderophore
ISSN:	1097-4164, 1097-4164
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Shrnutí:	Initiation is the rate-limiting step of translation, and in bacteria, mRNA secondary structure has been extensively reported as limiting the efficiency of translation by occluding the ribosome-binding site. In striking contrast with this inhibitory effect, we report here that stem-loop structures located within coding sequences instead activate translation initiation of the Escherichia coli fepA and bamA mRNAs involved in iron acquisition and outer membrane proteins assembly, respectively. Both structures promote ribosome binding in vitro, independently of their nucleotide sequence. Moreover, two small regulatory RNAs, OmrA and OmrB, base pair to and most likely disrupt the fepA stem-loop structure, thereby repressing FepA synthesis. By expanding our understanding of how mRNA cis-acting elements regulate translation, these data challenge the widespread view of mRNA secondary structures as translation inhibitors and show that translation-activating elements embedded in coding sequences can be targeted by small RNAs to inhibit gene expression.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1097-4164 1097-4164
DOI:	10.1016/j.molcel.2017.08.015