2gio: Difference between revisions

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New page: left|200px<br /><applet load="2gio" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gio" /> '''Solution Structure of a portion of the 5'UTR...
 
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==Overview==
==Overview==
Regulatory RNA elements, like riboswitches, respond to intracellular, signals by three-dimensional (3D) conformational changes. RNA thermometers, employ a similar strategy to sense temperature changes in the cell and, regulate the translational machinery. We present here the first 3D NMR, structure of the functional domain of a highly conserved bacterial RNA, thermometer containing the ribosome binding site that remains occluded at, normal temperatures (30 degrees C). We identified a region adjacent to the, Shine-Dalgarno sequence that has a network of weak hydrogen bonds within, the RNA helix. With the onset of heat shock at 42 degrees C, destabilisation of the RNA structure initiates at this region and favours, the release of the ribosome binding site and of the start codon. Deletion, of a highly conserved G residue leads to the formation of a stable regular, RNA helix that loses thermosensing ability. Our results indicate that RNA, thermometers are able to sense temperature changes without the aid of, accessory factors.
Regulatory RNA elements, like riboswitches, respond to intracellular signals by three-dimensional (3D) conformational changes. RNA thermometers employ a similar strategy to sense temperature changes in the cell and regulate the translational machinery. We present here the first 3D NMR structure of the functional domain of a highly conserved bacterial RNA thermometer containing the ribosome binding site that remains occluded at normal temperatures (30 degrees C). We identified a region adjacent to the Shine-Dalgarno sequence that has a network of weak hydrogen bonds within the RNA helix. With the onset of heat shock at 42 degrees C, destabilisation of the RNA structure initiates at this region and favours the release of the ribosome binding site and of the start codon. Deletion of a highly conserved G residue leads to the formation of a stable regular RNA helix that loses thermosensing ability. Our results indicate that RNA thermometers are able to sense temperature changes without the aid of accessory factors.


==About this Structure==
==About this Structure==
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Molecular basis for temperature sensing by an RNA thermometer., Chowdhury S, Maris C, Allain FH, Narberhaus F, EMBO J. 2006 Jun 7;25(11):2487-97. Epub 2006 May 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16710302 16710302]
Molecular basis for temperature sensing by an RNA thermometer., Chowdhury S, Maris C, Allain FH, Narberhaus F, EMBO J. 2006 Jun 7;25(11):2487-97. Epub 2006 May 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16710302 16710302]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Allain, F.H.]]
[[Category: Allain, F H.]]
[[Category: Chowdhury, S.]]
[[Category: Chowdhury, S.]]
[[Category: Maris, C.]]
[[Category: Maris, C.]]
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[[Category: g-g non cannonical pair]]
[[Category: g-g non cannonical pair]]


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Revision as of 18:32, 21 February 2008

File:2gio.gif


2gio

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Solution Structure of a portion of the 5'UTR of HspA mRNA of Bradyrhizobium japonicum

OverviewOverview

Regulatory RNA elements, like riboswitches, respond to intracellular signals by three-dimensional (3D) conformational changes. RNA thermometers employ a similar strategy to sense temperature changes in the cell and regulate the translational machinery. We present here the first 3D NMR structure of the functional domain of a highly conserved bacterial RNA thermometer containing the ribosome binding site that remains occluded at normal temperatures (30 degrees C). We identified a region adjacent to the Shine-Dalgarno sequence that has a network of weak hydrogen bonds within the RNA helix. With the onset of heat shock at 42 degrees C, destabilisation of the RNA structure initiates at this region and favours the release of the ribosome binding site and of the start codon. Deletion of a highly conserved G residue leads to the formation of a stable regular RNA helix that loses thermosensing ability. Our results indicate that RNA thermometers are able to sense temperature changes without the aid of accessory factors.

About this StructureAbout this Structure

2GIO is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

ReferenceReference

Molecular basis for temperature sensing by an RNA thermometer., Chowdhury S, Maris C, Allain FH, Narberhaus F, EMBO J. 2006 Jun 7;25(11):2487-97. Epub 2006 May 18. PMID:16710302

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