Crystal structure of GCN5 PCAF N-terminal domain reveals atypical ubiquitin ligase structure.


Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
23 10 2020
Historique:
received: 12 03 2020
revised: 22 07 2020
pubmed: 21 8 2020
medline: 10 3 2021
entrez: 22 8 2020
Statut: ppublish

Résumé

General control nonderepressible 5 (GCN5, also known as Kat2a) and p300/CBP-associated factor (PCAF, also known as Kat2b) are two homologous acetyltransferases. Both proteins share similar domain architecture consisting of a PCAF N-terminal (PCAF_N) domain, acetyltransferase domain, and a bromodomain. PCAF also acts as a ubiquitin E3 ligase whose activity is attributable to the PCAF_N domain, but its structural aspects are largely unknown. Here, we demonstrated that GCN5 exhibited ubiquitination activity in a similar manner to PCAF and its activity was supported by the ubiquitin-conjugating enzyme UbcH5. Moreover, we determined the crystal structure of the PCAF_N domain at 1.8 Å resolution and found that PCAF_N domain folds into a helical structure with a characteristic binuclear zinc region, which was not predicted from sequence analyses. The zinc region is distinct from known E3 ligase structures, suggesting this region may form a new class of E3 ligase. Our biochemical and structural study provides new insight into not only the functional significance of GCN5 but also into ubiquitin biology.

Identifiants

pubmed: 32820047
pii: S0021-9258(17)49341-0
doi: 10.1074/jbc.RA120.013431
pmc: PMC7586209
pii:
doi:

Substances chimiques

p300-CBP Transcription Factors EC 2.3.1.48
p300-CBP-associated factor EC 2.3.1.48
Ubiquitin-Protein Ligases EC 2.3.2.27

Banques de données

PDB
['2y0n', '7BY1']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

14630-14639

Informations de copyright

© 2020 Toma-Fukai et al.

Déclaration de conflit d'intérêts

Conflict of interest—All authors declare no conflict of interest in this work.

Références

Nucleic Acids Res. 2016 Jul 8;44(W1):W351-5
pubmed: 27131377
Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55
pubmed: 15299926
Biophys J. 1999 Jun;76(6):2879-86
pubmed: 10354416
Nature. 2008 Sep 18;455(7211):358-62
pubmed: 18758443
Nat Rev Mol Cell Biol. 2009 Nov;10(11):755-64
pubmed: 19851334
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
pubmed: 15572765
Nucleic Acids Res. 2015 Jan;43(Database issue):D364-8
pubmed: 25352545
Nature. 2020 Jan;577(7792):711-716
pubmed: 31969704
Cell. 2012 Mar 30;149(1):214-31
pubmed: 22464331
Nucleic Acids Res. 2019 Jan 8;47(D1):D427-D432
pubmed: 30357350
Nat Cell Biol. 2007 Mar;9(3):331-8
pubmed: 17293853
Mol Syst Biol. 2011 Oct 11;7:539
pubmed: 21988835
PLoS One. 2008 Jan 23;3(1):e1487
pubmed: 18213395
Microbiol Mol Biol Rev. 2000 Jun;64(2):435-59
pubmed: 10839822
Cell. 1996 Mar 22;84(6):843-51
pubmed: 8601308
Nature. 2007 Jun 28;447(7148):1135-8
pubmed: 17597759
J Biol Chem. 1999 Feb 26;274(9):5895-900
pubmed: 10026213
Nature. 2020 Jan;577(7792):717-720
pubmed: 31969703
Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):2023-30
pubmed: 14573958
Nat Commun. 2016 Nov 22;7:13147
pubmed: 27874008
Nat Struct Mol Biol. 2011 Feb;18(2):142-9
pubmed: 21217699
Oncogene. 2007 Aug 13;26(37):5341-57
pubmed: 17694077
Nat Rev Mol Cell Biol. 2016 Oct;17(10):626-42
pubmed: 27485899
Mol Cell Biol. 1998 Oct;18(10):5659-69
pubmed: 9742083
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32
pubmed: 20124692
Biopolymers. 1983 Dec;22(12):2577-637
pubmed: 6667333
Proteins. 2007 Jul 1;68(1):403-7
pubmed: 17410582
Cell Death Differ. 2013 Dec;20(12):1688-97
pubmed: 24013724
Int J Cell Biol. 2017;2017:8093813
pubmed: 28286521
Biochim Biophys Acta. 2004 Nov 29;1695(1-3):55-72
pubmed: 15571809
Nucleic Acids Res. 1998 Jun 15;26(12):2948-54
pubmed: 9611240

Auteurs

Sachiko Toma-Fukai (S)

Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.

Ryota Hibi (R)

Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.

Takao Naganuma (T)

Department of Molecular Metabolic Regulation, Diabetes Research Center, Research Institute, National Center for Global Health and Medicine, Shinjyuku-ku, Tokyo, Japan.

Mashito Sakai (M)

Department of Molecular Metabolic Regulation, Diabetes Research Center, Research Institute, National Center for Global Health and Medicine, Shinjyuku-ku, Tokyo, Japan.

Shinya Saijo (S)

Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki, Japan.

Nobutaka Shimizu (N)

Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki, Japan.

Michihiro Matsumoto (M)

Department of Molecular Metabolic Regulation, Diabetes Research Center, Research Institute, National Center for Global Health and Medicine, Shinjyuku-ku, Tokyo, Japan.

Toshiyuki Shimizu (T)

Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan. Electronic address: shimizu@mol.f.u-tokyo.ac.jp.

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Classifications MeSH