Evidence map›Paper›PMID 36993468›Full record

ArticlebioRxiv : the preprint server for biology2023

Cryo-EM structure of the human Sirtuin 6-nucleosome complex.

Un Seng Chio, Othman Rechiche, Alysia R Bryll, Jiang Zhu, Jessica L Feldman, Craig L Peterson, Song Tan, Jean-Paul Armache

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Un Seng ChioCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
Othman RechicheCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
Alysia R BryllProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Jiang ZhuCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
Jessica L FeldmanProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Craig L PetersonProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Song TanCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
Jean-Paul ArmacheCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
Pennsylvania State University · USUniversity of Massachusetts Chan Medical School · US

Funding

Regulation of chromatin dynamicsR35GM122519 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Craig L Peterson · 2017 to 2026
$9.2M
ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
Structural studies of chromatin complexesR35GM127034 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI SONG TAN · 2018 to 2026
$4.8M
Molecular mechanisms of the ACF chromatin remodeling complexF32GM137463 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHIO, UN SENG · 2020 to 2022
$201k
NIGMS NIH HHS F32 GM137463NIGMS NIH HHS R01 GM129325NIGMS NIH HHS R35 GM122519NIGMS NIH HHS R35 GM127034
6 · The paper itself

Abstract

Sirtuin 6 (SIRT6) is a multifaceted protein deacetylase/deacylase and a major target for small-molecule modulators of longevity and cancer. In the context of chromatin, SIRT6 removes acetyl groups from histone H3 in nucleosomes, but the molecular basis for its nucleosomal substrate preference is unknown. Our cryo-electron microscopy structure of human SIRT6 in complex with the nucleosome shows that the catalytic domain of SIRT6 pries DNA from the nucleosomal entry-exit site and exposes the histone H3 N-terminal helix, while the SIRT6 zinc-binding domain binds to the histone acidic patch using an arginine anchor. In addition, SIRT6 forms an inhibitory interaction with the C-terminal tail of histone H2A. The structure provides insights into how SIRT6 can deacetylate both H3 K9 and H3 K56. Teaser: The structure of the SIRT6 deacetylase/nucleosome complex suggests how the enzyme acts on both histone H3 K9 and K56 residues.

Identifiers

PMID36993468
PMCPMC10055229
OpenAlexW4327861800

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.