1nyh: Difference between revisions

Revision as of 15:11, 21 February 2008

Crystal Structure of the Coiled-coil Dimerization Motif of Sir4

OverviewOverview

The yeast silent information regulators Sir2, Sir3, and Sir4 physically interact with one another to establish a transcriptionally silent state by forming repressive chromatin structures. The Sir4 protein contains binding sites for both Sir2 and Sir3, and these protein-protein interactions are required for gene silencing. Here, we report the X-ray structure of the coiled-coil dimerization motif within the C-terminus of Sir4 and show that it forms a stable 1:1 complex with a dimeric fragment of Sir3 (residues 464-978). We have identified a cluster of residues on the surface of the Sir4 coiled coil required for specific interactions with Sir3. The histone deacetylase Sir2 can also bind to this complex, forming a ternary complex with the truncated Sir3 and Sir4 proteins. The dual interactions of Sir4 with Sir3 and Sir2 suggest a physical basis for recruiting Sir3 to chromatin by virtue of its interactions with Sir4 and with deacetylated histones in chromatin.

About this StructureAbout this Structure

1NYH is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the coiled-coil dimerization motif of Sir4 and its interaction with Sir3., Chang JF, Hall BE, Tanny JC, Moazed D, Filman D, Ellenberger T, Structure. 2003 Jun;11(6):637-49. PMID:12791253

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-[[Image:1nyh.jpg|left|200px]]<br /><applet load="1nyh" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nyh.jpg|left|200px]]<br /><applet load="1nyh" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nyh, resolution 3.10&Aring;" />
 '''Crystal Structure of the Coiled-coil Dimerization Motif of Sir4'''<br />
 ==Overview==
-The yeast silent information regulators Sir2, Sir3, and Sir4 physically, interact with one another to establish a transcriptionally silent state by, forming repressive chromatin structures. The Sir4 protein contains binding, sites for both Sir2 and Sir3, and these protein-protein interactions are, required for gene silencing. Here, we report the X-ray structure of the, coiled-coil dimerization motif within the C-terminus of Sir4 and show that, it forms a stable 1:1 complex with a dimeric fragment of Sir3 (residues, 464-978). We have identified a cluster of residues on the surface of the, Sir4 coiled coil required for specific interactions with Sir3. The histone, deacetylase Sir2 can also bind to this complex, forming a ternary complex, with the truncated Sir3 and Sir4 proteins. The dual interactions of Sir4, with Sir3 and Sir2 suggest a physical basis for recruiting Sir3 to, chromatin by virtue of its interactions with Sir4 and with deacetylated, histones in chromatin.
+The yeast silent information regulators Sir2, Sir3, and Sir4 physically interact with one another to establish a transcriptionally silent state by forming repressive chromatin structures. The Sir4 protein contains binding sites for both Sir2 and Sir3, and these protein-protein interactions are required for gene silencing. Here, we report the X-ray structure of the coiled-coil dimerization motif within the C-terminus of Sir4 and show that it forms a stable 1:1 complex with a dimeric fragment of Sir3 (residues 464-978). We have identified a cluster of residues on the surface of the Sir4 coiled coil required for specific interactions with Sir3. The histone deacetylase Sir2 can also bind to this complex, forming a ternary complex with the truncated Sir3 and Sir4 proteins. The dual interactions of Sir4 with Sir3 and Sir2 suggest a physical basis for recruiting Sir3 to chromatin by virtue of its interactions with Sir4 and with deacetylated histones in chromatin.
 ==About this Structure==
-NYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NYH OCA].
+NYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYH OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Chang, J.F.]]
+[[Category: Chang, J F.]]
 [[Category: Ellenberger, T.]]
 [[Category: Filman, D.]]
-[[Category: Hall, B.E.]]
+[[Category: Hall, B E.]]
 [[Category: Moazed, D.]]
-[[Category: Tanny, J.C.]]
+[[Category: Tanny, J C.]]
 [[Category: coiled-coil]]
 [[Category: repressor]]
 [[Category: transcription regulation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:39:39 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:25 2008''