Publications
2010
Giuliodori A M, Pietro F Di, Marzi S, Masquida B, Wagner R, Romby P, Gualerzi C O, Pon C L
The cspA mRNA is a thermosensor that modulates translation of the cold-shock protein CspA Journal Article
In: Mol Cell, vol. 37, no. 1, pp. 21-33, 2010, ISBN: 20129052, (1097-4164 (Electronic) 1097-2765 (Linking) Journal Article Research Support, Non-U.S. Gov't).
Abstract | Links | BibTeX | Tags: 5' Untranslated Regions Acclimatization *Cold Temperature Escherichia coli/*genetics/metabolism Escherichia coli Proteins/genetics/*physiology Gene Expression Regulation, Bacterial Heat-Shock Proteins/genetics/*physiology Models, Genetic Nucleic Acid Conformation *Protein Biosynthesis RNA, Messenger/chemistry/*physiology, ROMBY, Unité ARN, WESTHOF
@article{,
title = {The cspA mRNA is a thermosensor that modulates translation of the cold-shock protein CspA},
author = {A M Giuliodori and F Di Pietro and S Marzi and B Masquida and R Wagner and P Romby and C O Gualerzi and C L Pon},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=20129052},
isbn = {20129052},
year = {2010},
date = {2010-01-01},
journal = {Mol Cell},
volume = {37},
number = {1},
pages = {21-33},
abstract = {Cold induction of cspA, the paradigm Escherichia coli cold-shock gene, is mainly subject to posttranscriptional control, partly promoted by cis-acting elements of its transcript, whose secondary structure at 37 degrees C and at cold-shock temperature has been elucidated here by enzymatic and chemical probing. The structures, which were also validated by mutagenesis, demonstrate that cspA mRNA undergoes a temperature-dependent structural rearrangement, likely resulting from stabilization in the cold of an otherwise thermodynamically unstable folding intermediate. At low temperature, the "cold-shock" structure is more efficiently translated and somewhat less susceptible to degradation than the 37 degrees C structure. Overall, our data shed light on a molecular mechanism at the basis of the cold-shock response, indicating that cspA mRNA is able to sense temperature downshifts, adopting functionally distinct structures at different temperatures, even without the aid of trans-acting factors. Unlike with other previously studied RNA thermometers, these structural rearrangements do not result from melting of hairpin structures.},
note = {1097-4164 (Electronic)
1097-2765 (Linking)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {5' Untranslated Regions Acclimatization *Cold Temperature Escherichia coli/*genetics/metabolism Escherichia coli Proteins/genetics/*physiology Gene Expression Regulation, Bacterial Heat-Shock Proteins/genetics/*physiology Models, Genetic Nucleic Acid Conformation *Protein Biosynthesis RNA, Messenger/chemistry/*physiology, ROMBY, Unité ARN, WESTHOF},
pubstate = {published},
tppubtype = {article}
}