Proteopedia

8eu9

Class1 of the INO80-Nucleosome complexClass1 of the INO80-Nucleosome complex

Structural highlights

8eu9 is a 10 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:Electron Microscopy, Resolution 3.48Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

INO80_YEAST ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair (PubMed:10952318, PubMed:12887900). Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates (PubMed:10952318, PubMed:10361278). The INO80 complex is involved in DNA repair by associating with 'Ser-129' phosphorylated H2A histones as a response to DNA damage (PubMed:15607974, PubMed:15607975).[1] [2] [3] [4] [5]

Publication Abstract from PubMed

Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report structures of Saccharomyces cerevisiae INO80 bound to a hexasome or a nucleosome. INO80 binds the two substrates in substantially different orientations. On a hexasome, INO80 places its ATPase subunit, Ino80, at superhelical location -2 (SHL -2), in contrast to SHL -6 and SHL -7, as previously seen on nucleosomes. Our results suggest that INO80 action on hexasomes resembles action by other remodelers on nucleosomes such that Ino80 is maximally active near SHL -2. The SHL -2 position also plays a critical role for nucleosome remodeling by INO80. Overall, the mechanistic adaptations used by INO80 for preferential hexasome sliding imply that subnucleosomal particles play considerable regulatory roles.

Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility.,Wu H, Munoz EN, Hsieh LJ, Chio US, Gourdet MA, Narlikar GJ, Cheng Y Science. 2023 Jul 21;381(6655):319-324. doi: 10.1126/science.adf4197. Epub 2023 , Jun 29. PMID:37384669[6]

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

References

  1. ↑ Ebbert R, Birkmann A, Schuller HJ. The product of the SNF2/SWI2 paralogue INO80 of Saccharomyces cerevisiae required for efficient expression of various yeast structural genes is part of a high-molecular-weight protein complex. Mol Microbiol. 1999 May;32(4):741-51. PMID:10361278
  2. ↑ Shen X, Mizuguchi G, Hamiche A, Wu C. A chromatin remodelling complex involved in transcription and DNA processing. Nature. 2000 Aug 3;406(6795):541-4. PMID:10952318 doi:http://dx.doi.org/10.1038/35020123
  3. ↑ Shen X, Ranallo R, Choi E, Wu C. Involvement of actin-related proteins in ATP-dependent chromatin remodeling. Mol Cell. 2003 Jul;12(1):147-55. PMID:12887900
  4. ↑ Morrison AJ, Highland J, Krogan NJ, Arbel-Eden A, Greenblatt JF, Haber JE, Shen X. INO80 and gamma-H2AX interaction links ATP-dependent chromatin remodeling to DNA damage repair. Cell. 2004 Dec 17;119(6):767-75. doi: 10.1016/j.cell.2004.11.037. PMID:15607974 doi:http://dx.doi.org/10.1016/j.cell.2004.11.037
  5. ↑ van Attikum H, Fritsch O, Hohn B, Gasser SM. Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair. Cell. 2004 Dec 17;119(6):777-88. doi: 10.1016/j.cell.2004.11.033. PMID:15607975 doi:http://dx.doi.org/10.1016/j.cell.2004.11.033
  6. ↑ Wu H, Muñoz EN, Hsieh LJ, Chio US, Gourdet MA, Narlikar GJ, Cheng Y. Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility. Science. 2023 Jun 28. PMID:37384669 doi:10.1126/science.adf4197

8eu9, resolution 3.48Å

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