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==Crystal Structure of Elp2==
==Crystal Structure of Elp2==
<StructureSection load='4xfv' size='340' side='right' caption='[[4xfv]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='4xfv' size='340' side='right'caption='[[4xfv]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4xfv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XFV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XFV FirstGlance]. <br>
<table><tr><td colspan='2'>[[4xfv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XFV FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xfv OCA], [http://pdbe.org/4xfv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xfv RCSB], [http://www.ebi.ac.uk/pdbsum/4xfv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xfv ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xfv OCA], [https://pdbe.org/4xfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xfv RCSB], [https://www.ebi.ac.uk/pdbsum/4xfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xfv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ELP2_YEAST ELP2_YEAST]] Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling. It acetylates histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8'. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitiviy to Pichia inositovora toxin. May be involved in tRNA modification. ELP2 is dispensable for the complex integrity and, in vitro, is not required for complex HAT activity. It is not required for the association of the complex with nascent RNA transcript. Independently, ELP2 may be involved in polarized exocytosis. Is required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA.<ref>PMID:10024884</ref> <ref>PMID:11296232</ref> <ref>PMID:11689709</ref> <ref>PMID:11904415</ref> <ref>PMID:13680368</ref> <ref>PMID:15138274</ref> <ref>PMID:15769872</ref> <ref>PMID:15780940</ref>
[https://www.uniprot.org/uniprot/ELP2_YEAST ELP2_YEAST] Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling. It acetylates histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8'. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitiviy to Pichia inositovora toxin. May be involved in tRNA modification. ELP2 is dispensable for the complex integrity and, in vitro, is not required for complex HAT activity. It is not required for the association of the complex with nascent RNA transcript. Independently, ELP2 may be involved in polarized exocytosis. Is required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA.<ref>PMID:10024884</ref> <ref>PMID:11296232</ref> <ref>PMID:11689709</ref> <ref>PMID:11904415</ref> <ref>PMID:13680368</ref> <ref>PMID:15138274</ref> <ref>PMID:15769872</ref> <ref>PMID:15780940</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dong, C]]
[[Category: Large Structures]]
[[Category: Lin, Z]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Long, J]]
[[Category: Dong C]]
[[Category: Shen, Y]]
[[Category: Lin Z]]
[[Category: Elongator complex]]
[[Category: Long J]]
[[Category: Elp2]]
[[Category: Shen Y]]
[[Category: Translation]]

Latest revision as of 18:27, 8 November 2023

Crystal Structure of Elp2Crystal Structure of Elp2

Structural highlights

4xfv is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ELP2_YEAST Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling. It acetylates histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8'. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitiviy to Pichia inositovora toxin. May be involved in tRNA modification. ELP2 is dispensable for the complex integrity and, in vitro, is not required for complex HAT activity. It is not required for the association of the complex with nascent RNA transcript. Independently, ELP2 may be involved in polarized exocytosis. Is required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA.[1] [2] [3] [4] [5] [6] [7] [8]

Publication Abstract from PubMed

Elongator is a highly conserved multiprotein complex composed of six subunits (Elp1-6). Elongator has been associated with various cellular activities and has attracted clinical attention because of its role in certain neurodegenerative diseases. Here, we present the crystal structure of the Elp2 subunit revealing two seven-bladed WD40 beta propellers, and show by structure-guided mutational analyses that the WD40 fold integrity of Elp2 is necessary for its binding to Elp1 and Elp3 subunits in multiple species. The detailed biochemical experiments indicate that Elp2 binds microtubules through its conserved alkaline residues in vitro and in vivo. We find that both the mutually independent Elp2-mediated Elongator assembly and the cytoskeleton association are important for yeast viability. In addition, mutation of Elp2 greatly affects the histone H3 acetylation activity of Elongator in vivo. Our results indicate that Elp2 is a necessary component for functional Elongator and acts as a hub in the formation of various complexes.

The Elp2 Subunit Is Essential for Elongator Complex Assembly and Functional Regulation.,Dong C, Lin Z, Diao W, Li D, Chu X, Wang Z, Zhou H, Xie Z, Shen Y, Long J Structure. 2015 Apr 29. pii: S0969-2126(15)00122-7. doi:, 10.1016/j.str.2015.03.018. PMID:25960406[9]

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

References

  1. ↑ Otero G, Fellows J, Li Y, de Bizemont T, Dirac AM, Gustafsson CM, Erdjument-Bromage H, Tempst P, Svejstrup JQ. Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Mol Cell. 1999 Jan;3(1):109-18. PMID:10024884
  2. ↑ Frohloff F, Fichtner L, Jablonowski D, Breunig KD, Schaffrath R. Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin. EMBO J. 2001 Apr 17;20(8):1993-2003. PMID:11296232 doi:10.1093/emboj/20.8.1993
  3. ↑ Krogan NJ, Greenblatt JF. Characterization of a six-subunit holo-elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae. Mol Cell Biol. 2001 Dec;21(23):8203-12. PMID:11689709 doi:10.1128/MCB.21.23.8203-8212.2001
  4. ↑ Winkler GS, Kristjuhan A, Erdjument-Bromage H, Tempst P, Svejstrup JQ. Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3517-22. PMID:11904415 doi:10.1073/pnas.022042899
  5. ↑ Klassen R, Meinhardt F. Structural and functional analysis of the killer element pPin1-3 from Pichia inositovora. Mol Genet Genomics. 2003 Nov;270(2):190-9. Epub 2003 Sep 9. PMID:13680368 doi:10.1007/s00438-003-0920-5
  6. ↑ Petrakis TG, Wittschieben BO, Svejstrup JQ. Molecular architecture, structure-function relationship, and importance of the Elp3 subunit for the RNA binding of holo-elongator. J Biol Chem. 2004 Jul 30;279(31):32087-92. Epub 2004 May 11. PMID:15138274 doi:10.1074/jbc.M403361200
  7. ↑ Huang B, Johansson MJ, Bystrom AS. An early step in wobble uridine tRNA modification requires the Elongator complex. RNA. 2005 Apr;11(4):424-36. PMID:15769872 doi:11/4/424
  8. ↑ Rahl PB, Chen CZ, Collins RN. Elp1p, the yeast homolog of the FD disease syndrome protein, negatively regulates exocytosis independently of transcriptional elongation. Mol Cell. 2005 Mar 18;17(6):841-53. PMID:15780940 doi:http://dx.doi.org/S1097-2765(05)01117-2
  9. ↑ Dong C, Lin Z, Diao W, Li D, Chu X, Wang Z, Zhou H, Xie Z, Shen Y, Long J. The Elp2 Subunit Is Essential for Elongator Complex Assembly and Functional Regulation. Structure. 2015 Apr 29. pii: S0969-2126(15)00122-7. doi:, 10.1016/j.str.2015.03.018. PMID:25960406 doi:http://dx.doi.org/10.1016/j.str.2015.03.018

4xfv, resolution 3.20Å

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