Novel role for a bacterial nucleoid protein in translation of mRNAs with suboptimal ribosome-binding sites.
In Escherichia coli, the major nucleoid protein H-NS limits transcription by acting as a repressor or transcriptional silencer, presumably by its ability to close the looped chromosome domains in the nucleoid through DNA-protein-DNA bridging. Here, we demonstrate the direct involvement of H-NS as a positive factor stimulating translation of the malT mRNA. In vitro studies showed that H-NS facilitates a repositioning of the 30S preinitiation complex on the malT mRNA. H-NS stimulation of translation depended on the AU-rich -35 to -40 region of the mRNA. Several additional examples were found demonstrating a novel function for H-NS in translation of genes with suboptimal ribosome-binding sequences.
Park
Hyun-Sook
HS
Department of Molecular Biology, Umeå Centre for Microbial Research (UCMR), Umeå University, Umeå, Sweden. hyun-sook.park@molbiol.umu.se
Ostberg
Yngve
Y
Johansson
Jörgen
J
Wagner
E Gerhart H
EG
Uhlin
Bernt Eric
BE
D001665:Binding Sites; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D036781:Fimbriae Proteins / Q000378:metabolism*; D011485:Protein Binding; D014176:Protein Biosynthesis; D012270:Ribosomes / Q000378:metabolism*; D015533:Transcriptional Activation
D029968:Escherichia coli Proteins; C529458:FimG protein, E coli; D036781:Fimbriae Proteins