RRC ID |
53694
|
Author |
Benhalevy D, Bochkareva ES, Biran I, Bibi E.
|
Title |
Model Uracil-Rich RNAs and Membrane Protein mRNAs Interact Specifically with Cold Shock Proteins in Escherichia coli.
|
Journal |
PLoS One
|
Abstract |
Are integral membrane protein-encoding mRNAs (MPRs) different from other mRNAs such as those encoding cytosolic mRNAs (CPRs)? This is implied from the emerging concept that MPRs are specifically recognized and delivered to membrane-bound ribosomes in a translation-independent manner. MPRs might be recognized through uracil-rich segments that encode hydrophobic transmembrane helices. To investigate this hypothesis, we designed DNA sequences encoding model untranslatable transcripts that mimic MPRs or CPRs. By utilizing in vitro-synthesized biotinylated RNAs mixed with Escherichia coli extracts, we identified a highly specific interaction that takes place between transcripts that mimic MPRs and the cold shock proteins CspE and CspC, which are normally expressed under physiological conditions. Co-purification studies with E. coli expressing 6His-tagged CspE or CspC confirmed that the specific interaction occurs in vivo not only with the model uracil-rich untranslatable transcripts but also with endogenous MPRs. Our results suggest that the evolutionarily conserved cold shock proteins may have a role, possibly as promiscuous chaperons, in the biogenesis of MPRs.
|
Volume |
10(7)
|
Pages |
e0134413
|
Published |
2015-1-1
|
DOI |
10.1371/journal.pone.0134413
|
PII |
PONE-D-15-15350
|
PMID |
26225847
|
PMC |
PMC4520561
|
MeSH |
Cell Membrane / metabolism
Cold Shock Proteins and Peptides / metabolism*
Escherichia coli / metabolism*
Protein Binding
RNA, Bacterial / metabolism*
RNA, Messenger / metabolism
Uracil / metabolism*
|
IF |
2.74
|
Times Cited |
9
|
Resource |
Prokaryotes E. coli |
|