Structural and functional analysis of the SET3 histone deacetylase complex.


Journal

Acta crystallographica. Section F, Structural biology communications
ISSN: 2053-230X
Titre abrégé: Acta Crystallogr F Struct Biol Commun
Pays: United States
ID NLM: 101620319

Informations de publication

Date de publication:
01 Mar 2022
Historique:
received: 18 11 2021
accepted: 16 01 2022
entrez: 2 3 2022
pubmed: 3 3 2022
medline: 5 4 2022
Statut: ppublish

Résumé

The SET3 complex (SET3C) is a seven-subunit histone deacetylase complex that is capable of transcriptional regulation. Methylated histone 3 marks recruit SET3C to the nucleosome, and the SET3C catalytic subunits deacetylate the histone 3 and 4 tails. There is very limited structural knowledge of the SET3C subunits, with most subunits having unknown structures or functions. Here, a catalytically active SET3 complex was endogenously purified from Saccharomyces cerevisiae and utilized for negative-stain electron microscopy (EM) to determine an apo model for the holo complex. The negative-stain EM 3D model revealed a three-lobe architecture, with each lobe extending from a central point.

Identifiants

pubmed: 35234136
pii: S2053230X22000553
doi: 10.1107/S2053230X22000553
pmc: PMC8900736
doi:

Substances chimiques

Saccharomyces cerevisiae Proteins 0
Set3 protein, S cerevisiae EC 3.5.1.-
Histone Deacetylases EC 3.5.1.98

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

113-118

Subventions

Organisme : NIH HHS
ID : S10 OD026963
Pays : United States
Organisme : NIH HHS
ID : P01-CA092584
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM129325
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA060553
Pays : United States
Organisme : NIH HHS
ID : R01-GM135651
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008382
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM135651
Pays : United States
Organisme : NCI NIH HHS
ID : U54 CA193419
Pays : United States
Organisme : NIH HHS
ID : 1S10OD026963-01
Pays : United States
Organisme : NCI NIH HHS
ID : P01 CA092584
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM144559
Pays : United States

Références

Nucleic Acids Res. 2016 Jul 8;44(W1):W344-50
pubmed: 27166375
Nat Methods. 2017 Mar;14(3):290-296
pubmed: 28165473
Mol Cell. 2003 Mar;11(3):709-19
pubmed: 12667453
Protein J. 2018 Oct;37(5):391-406
pubmed: 30069656
Genes Dev. 2001 Nov 15;15(22):2991-3004
pubmed: 11711434
Protein Sci. 2021 Jan;30(1):70-82
pubmed: 32881101
Nucleic Acids Res. 2019 Jul 2;47(W1):W402-W407
pubmed: 31251384
Curr Opin Genet Dev. 2002 Apr;12(2):198-209
pubmed: 11893494
J Mol Biol. 2017 Jun 30;429(13):2066-2074
pubmed: 27697561
J Struct Biol. 2003 Sep;143(3):185-200
pubmed: 14572474
Bioinformatics. 2015 Mar 15;31(6):857-63
pubmed: 25391399
Nucleic Acids Res. 2020 Dec 2;48(21):12151-12168
pubmed: 33231641
Elife. 2016 Nov 15;5:
pubmed: 27845625
FEBS J. 2006 Jul;273(14):3121-35
pubmed: 16857008
Protein Sci. 2021 Jan;30(1):136-150
pubmed: 33030237
J Struct Biol. 2007 Jan;157(1):38-46
pubmed: 16859925
EMBO J. 2000 Jul 17;19(14):3739-49
pubmed: 10899127
Mol Cell Biol. 2011 Sep;31(17):3569-83
pubmed: 21709022
J Comput Chem. 2004 Oct;25(13):1605-12
pubmed: 15264254
Genes Dev. 1998 Mar 1;12(5):599-606
pubmed: 9499396
J Mol Biol. 1999 Sep 17;292(2):195-202
pubmed: 10493868
Genome Biol. 2005;6(8):227
pubmed: 16086857
J Struct Biol. 2009 May;166(2):205-13
pubmed: 19374019
Nature. 2020 Mar;579(7799):452-455
pubmed: 32188938
Eukaryot Cell. 2005 Jan;4(1):17-29
pubmed: 15643056
Nature. 2003 Oct 16;425(6959):737-41
pubmed: 14562106
J Biol Chem. 2019 Sep 20;294(38):13928-13938
pubmed: 31358618
Cell. 2009 Apr 17;137(2):259-72
pubmed: 19379692
Nature. 2021 Aug;596(7873):583-589
pubmed: 34265844
Trends Biochem Sci. 2010 Oct;35(10):565-74
pubmed: 20451393
J Mol Biol. 2005 Aug 26;351(4):923-35
pubmed: 16051270
Nat Commun. 2020 May 1;11(1):2181
pubmed: 32358498
Nucleic Acids Res. 2021 Jun 4;49(10):5502-5519
pubmed: 33963860
Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4152-7
pubmed: 9539705
Nucleic Acids Res. 2010 Jul;38(Web Server issue):W529-33
pubmed: 20478830
Biochemistry. 2004 Aug 31;43(34):11083-91
pubmed: 15323567
Genes Dev. 2001 Sep 15;15(18):2343-60
pubmed: 11562345
Nucleic Acids Res. 2021 Jan 8;49(D1):D412-D419
pubmed: 33125078
J Struct Biol. 2003 Jun;142(3):334-47
pubmed: 12781660
J Struct Biol. 2005 Jul;151(1):41-60
pubmed: 15890530
Science. 2002 Nov 15;298(5597):1412-4
pubmed: 12434058
J Struct Biol. 2007 Jan;157(1):281-7
pubmed: 16963278
Protein Sci. 2018 Jan;27(1):14-25
pubmed: 28710774

Auteurs

Alexis A Reyes (AA)

Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.

Susan Fishbain (S)

Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.

Yuan He (Y)

Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.

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Classifications MeSH