1auu

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(New page: 200px<br /><applet load="1auu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1auu" /> '''SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN...)
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[[Image:1auu.gif|left|200px]]<br /><applet load="1auu" size="350" color="white" frame="true" align="right" spinBox="true"
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'''SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES'''<br />
'''SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES'''<br />
==Overview==
==Overview==
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SacY is the prototype of a family of regulatory proteins able to prevent, transcription termination. It interacts with a 29 nucleotide RNA sequence, able to fold into a stem-loop structure and partially overlapping with a, terminator sequence located in the 5' leader mRNA region of the gene it, controls. We show here that the N-terminal fragment of SacY, SacY(1-55), and the corresponding fragments of other members of the family have, antiterminator activities with efficiency and specificity identical to, those of the full-length proteins. In vitro, this activity correlates with, the specific affinity of SacY(1-55) for its RNA target. UV melting, experiments demonstrate that SacY(1-55) binding stabilizes the RNA target, structure. The NMR solution structure of SacY(1-55) is very similar to, that obtained in the crystal (van Tilbeurgh et al., 1997): the peptide is, folded as a symmetrical dimer without any structural homology with other, RNA-binding domains yet characterized. According to a preliminary NMR, analysis of the SacY(1-55)-RNA complex, the protein dimer is not disrupted, upon RNA binding and several residues implicated in RNA recognition are, located at the edge of the dimer interface. This suggests a new mode of, protein-RNA interaction.
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SacY is the prototype of a family of regulatory proteins able to prevent transcription termination. It interacts with a 29 nucleotide RNA sequence able to fold into a stem-loop structure and partially overlapping with a terminator sequence located in the 5' leader mRNA region of the gene it controls. We show here that the N-terminal fragment of SacY, SacY(1-55), and the corresponding fragments of other members of the family have antiterminator activities with efficiency and specificity identical to those of the full-length proteins. In vitro, this activity correlates with the specific affinity of SacY(1-55) for its RNA target. UV melting experiments demonstrate that SacY(1-55) binding stabilizes the RNA target structure. The NMR solution structure of SacY(1-55) is very similar to that obtained in the crystal (van Tilbeurgh et al., 1997): the peptide is folded as a symmetrical dimer without any structural homology with other RNA-binding domains yet characterized. According to a preliminary NMR analysis of the SacY(1-55)-RNA complex, the protein dimer is not disrupted upon RNA binding and several residues implicated in RNA recognition are located at the edge of the dimer interface. This suggests a new mode of protein-RNA interaction.
==About this Structure==
==About this Structure==
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1AUU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AUU OCA].
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1AUU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUU OCA].
==Reference==
==Reference==
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[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:08:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:30 2008''

Revision as of 09:48, 21 February 2008


1auu

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SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES

Overview

SacY is the prototype of a family of regulatory proteins able to prevent transcription termination. It interacts with a 29 nucleotide RNA sequence able to fold into a stem-loop structure and partially overlapping with a terminator sequence located in the 5' leader mRNA region of the gene it controls. We show here that the N-terminal fragment of SacY, SacY(1-55), and the corresponding fragments of other members of the family have antiterminator activities with efficiency and specificity identical to those of the full-length proteins. In vitro, this activity correlates with the specific affinity of SacY(1-55) for its RNA target. UV melting experiments demonstrate that SacY(1-55) binding stabilizes the RNA target structure. The NMR solution structure of SacY(1-55) is very similar to that obtained in the crystal (van Tilbeurgh et al., 1997): the peptide is folded as a symmetrical dimer without any structural homology with other RNA-binding domains yet characterized. According to a preliminary NMR analysis of the SacY(1-55)-RNA complex, the protein dimer is not disrupted upon RNA binding and several residues implicated in RNA recognition are located at the edge of the dimer interface. This suggests a new mode of protein-RNA interaction.

About this Structure

1AUU is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins., Manival X, Yang Y, Strub MP, Kochoyan M, Steinmetz M, Aymerich S, EMBO J. 1997 Aug 15;16(16):5019-29. PMID:9305643

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