Is Thermosensing Property of RNA Thermometers Unique?

A large number of studies have been dedicated to identify the structural and sequence based features of RNA thermometers, mRNAs that regulate their translation initiation rate with temperature. It has been shown that the melting of the ribosome-binding site (RBS) plays a prominent role in this therm...

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Vydáno v:PloS one Ročník 5; číslo 7; s. e11308
Hlavní autoři: Shah, Premal, Gilchrist, Michael A.
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States Public Library of Science 02.07.2010
Public Library of Science (PLoS)
Témata:
Bacillus subtilis
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Binding sites
Bioinformatics
Biophysics/RNA Structure
Biophysics/Transcription and Translation
Computational Biology/Comparative Sequence Analysis
E coli
Escherichia coli
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Evolutionary biology
Gammaproteobacteria - genetics
Gammaproteobacteria - metabolism
Gene expression
Genomes
Genomics
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - metabolism
Melting
Messenger RNA
Mutation
Nucleic Acid Conformation
Nucleotide sequence
Probability
Prokaryotes
Proteobacteria
Ribonucleic acid
RNA
RNA, Bacterial - chemistry
RNA, Bacterial - metabolism
Sigma Factor - chemistry
Sigma Factor - metabolism
Software
Studies
Temperature
Thermometers
Translation (Genetics)
Translation initiation
United States > US
Tennessee
ISSN:1932-6203, 1932-6203
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Shrnutí:A large number of studies have been dedicated to identify the structural and sequence based features of RNA thermometers, mRNAs that regulate their translation initiation rate with temperature. It has been shown that the melting of the ribosome-binding site (RBS) plays a prominent role in this thermosensing process. However, little is known as to how widespread this melting phenomenon is as earlier studies on the subject have worked with a small sample of known RNA thermometers. We have developed a novel method of studying the melting of RNAs with temperature by computationally sampling the distribution of the RNA structures at various temperatures using the RNA folding software Vienna. In this study, we compared the thermosensing property of 100 randomly selected mRNAs and three well known thermometers--rpoH, ibpA and agsA sequences from E. coli. We also compared the rpoH sequences from 81 mesophilic proteobacteria. Although both rpoH and ibpA show a higher rate of melting at their RBS compared with the mean of non-thermometers, contrary to our expectations these higher rates are not significant. Surprisingly, we also do not find any significant differences between rpoH thermometers from other gamma-proteobacteria and E. coli non-thermometers.
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Conceived and designed the experiments: PS MAG. Performed the experiments: PS. Analyzed the data: PS MAG. Wrote the paper: PS.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0011308