5chl

From Proteopedia

(Difference between revisions)

Revision as of 11:38, 27 March 2020

Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex

Structural highlights

5chl is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VPS72_DROME] Part of the Tip60 chromatin-remodeling complex which is involved in DNA repair. Upon induction of DNA double-strand breaks, this complex acetylates phosphorylated H2AV in nucleosomes and exchanges it with unmodified H2AV.^[1] ^[2] [H2AZ_HUMAN] Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.^[3]

Publication Abstract from PubMed

Histone variant H2A.Z, a universal mark of dynamic nucleosomes flanking gene promoters and enhancers, is incorporated into chromatin by SRCAP (SWR1), an ATP-dependent, multicomponent chromatin-remodeling complex. The YL1 (Swc2) subunit of SRCAP (SWR1) plays an essential role in H2A.Z recognition, but how it achieves this has been unclear. Here, we report the crystal structure of the H2A.Z-binding domain of Drosophila melanogaster YL1 (dYL1-Z) in complex with an H2A.Z-H2B dimer at 1.9-A resolution. The dYL1-Z domain adopts a new whip-like structure that wraps over H2A.Z-H2B, and preferential recognition is largely conferred by three residues in loop 2, the hyperacidic patch and the extended alphaC helix of H2A.Z. Importantly, this domain is essential for deposition of budding yeast H2A.Z in vivo and SRCAP (SWR1)-catalyzed histone H2A.Z replacement in vitro. Our studies distinguish YL1-Z from known H2A.Z chaperones and suggest a hierarchical mechanism based on increasing binding affinity facilitating H2A.Z transfer from SRCAP (SWR1) to the nucleosome.

Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1.,Liang X, Shan S, Pan L, Zhao J, Ranjan A, Wang F, Zhang Z, Huang Y, Feng H, Wei D, Huang L, Liu X, Zhong Q, Lou J, Li G, Wu C, Zhou Z Nat Struct Mol Biol. 2016 Apr;23(4):317-23. doi: 10.1038/nsmb.3190. Epub 2016 Mar, 14. PMID:26974124^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kusch T, Florens L, Macdonald WH, Swanson SK, Glaser RL, Yates JR 3rd, Abmayr SM, Washburn MP, Workman JL. Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions. Science. 2004 Dec 17;306(5704):2084-7. Epub 2004 Nov 4. PMID:15528408 doi:http://dx.doi.org/1103455
↑ Wu WH, Alami S, Luk E, Wu CH, Sen S, Mizuguchi G, Wei D, Wu C. Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nat Struct Mol Biol. 2005 Dec;12(12):1064-71. Epub 2005 Nov 20. PMID:16299513 doi:http://dx.doi.org/nsmb1023
↑ Farris SD, Rubio ED, Moon JJ, Gombert WM, Nelson BH, Krumm A. Transcription-induced chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z. J Biol Chem. 2005 Jul 1;280(26):25298-303. Epub 2005 May 6. PMID:15878876 doi:http://dx.doi.org/10.1074/jbc.M501784200
↑ Liang X, Shan S, Pan L, Zhao J, Ranjan A, Wang F, Zhang Z, Huang Y, Feng H, Wei D, Huang L, Liu X, Zhong Q, Lou J, Li G, Wu C, Zhou Z. Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1. Nat Struct Mol Biol. 2016 Apr;23(4):317-23. doi: 10.1038/nsmb.3190. Epub 2016 Mar, 14. PMID:26974124 doi:http://dx.doi.org/10.1038/nsmb.3190

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5chl"

@@ Line 1: / Line 1: @@
 ==Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex==
-<StructureSection load='5chl' size='340' side='right' caption='[[5chl]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
+<StructureSection load='5chl' size='340' side='right'caption='[[5chl]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[5chl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CHL FirstGlance]. <br>
@@ Line 17: / Line 17: @@
 </div>
 <div class="pdbe-citations 5chl" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Liang, X]]
 [[Category: Pan, L]]

5chl

From Proteopedia

Revision as of 11:38, 27 March 2020

Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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