2c1j: Difference between revisions

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[[Image:2c1j.~~gif~~|left|200px]]

[[Image:2c1j.png|left|200px]]

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~~'''~~MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND PHOSPHOACETYLATED HISTONE H3 BY 14-3-3~~'''~~

===MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND PHOSPHOACETYLATED HISTONE H3 BY 14-3-3===

~~==Overview==~~

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~~Phosphorylation of histone H3 is implicated in transcriptional activation and chromosome condensation~~, ~~but its immediate molecular function has remained obscure. By affinity chromatography of nuclear extracts against modified H3 tail peptides~~, ~~we identified 14-3-3 isoforms~~ as ~~proteins that bind these tails in a strictly phosphorylation-dependent manner~~. ~~Acetylation of lysines 9 and 14 does not impede 14-3-3 binding to serine 10-phosphorylated H3 tails~~. ~~In vivo~~, ~~14-3-3~~ is ~~inducibly recruited to c-fos and c-jun nucleosomes upon gene activation, concomitant with H3 phosphoacetylation. We have determined~~ the ~~structures of 14-3-3zeta complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides~~. ~~These reveal a distinct mode of 14~~-3-3/phosphopeptide binding and provide a structural understanding for the lack of effect of acetylation at lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of proteins that mediate the effect of histone phosphorylation at inducible genes.

The line below this paragraph, {{ABSTRACT_PUBMED_16246723}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16246723 is the PubMed ID number.

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==About this Structure==

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[[Category: Phosphorylation]]

[[Category: Signaling protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 21~~:06:20 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:12:28 2008''

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-[[Image:2c1j.gif|left|200px]]
+{{Seed}}
+[[Image:2c1j.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2c1j|  PDB=2c1j  |  SCENE=  }}
-'''MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND PHOSPHOACETYLATED HISTONE H3 BY 14-3-3'''
+===MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND PHOSPHOACETYLATED HISTONE H3 BY 14-3-3===
-==Overview==
+<!--
-Phosphorylation of histone H3 is implicated in transcriptional activation and chromosome condensation, but its immediate molecular function has remained obscure. By affinity chromatography of nuclear extracts against modified H3 tail peptides, we identified 14-3-3 isoforms as proteins that bind these tails in a strictly phosphorylation-dependent manner. Acetylation of lysines 9 and 14 does not impede 14-3-3 binding to serine 10-phosphorylated H3 tails. In vivo, 14-3-3 is inducibly recruited to c-fos and c-jun nucleosomes upon gene activation, concomitant with H3 phosphoacetylation. We have determined the structures of 14-3-3zeta complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides. These reveal a distinct mode of 14-3-3/phosphopeptide binding and provide a structural understanding for the lack of effect of acetylation at lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of proteins that mediate the effect of histone phosphorylation at inducible genes.
+The line below this paragraph, {{ABSTRACT_PUBMED_16246723}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16246723 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16246723}}
 ==About this Structure==
@@ Line 41: / Line 45: @@
 [[Category: Phosphorylation]]
 [[Category: Signaling protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:06:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:12:28 2008''