Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Alternative catalytic residues in the active site of Esco acetyltransferases.

Scientific reports - 17 Jun 2020

Ajam Tahereh, De Inessa, Petkau Nikolai, Whelan Gabriela, Pena Vladimir, Eichele Gregor

Abstract excerpt

Cohesin is a protein complex whose core subunits, Smc1, Smc3, Scc1, and SA1/SA2 form a ring-like structure encircling the DNA. Cohesins play a key role in the expression, repair, and segregation of eukaryotic genomes. Following a catalytic mechanism that is insufficiently understood, Esco1 and Esco2 acetyltransferases acetylate the cohesin subunit Smc3, thereby inducing stabilization of cohesin on DNA. As a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biocatalysis
Share to Acetylation
Share to Acetyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amino Acid Sequence

Share to Catalytic Domain

Share to Chromosomal Proteins, Non-Histone

Share to Coenzyme A

Share to Models, Molecular

Source

Open in PubMed Open full text

Identifiers

PMID: 32555289
DOI: 10.1038/s41598-020-66795-z
PMCID: PMC7300003

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Alternative catalytic residues in the active site of Esco acetyltransferases.PMID 32555289Read ↗

Sister Chromatid Cohesion Establishment Factor ESCO1 Operates by Substrate-Assisted Catalysis.Semantic proximity Read ↗

Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases.Semantic proximity Read ↗

Closing the cohesin ring: structure and function of its Smc3-kleisin interface.Semantic proximity Read ↗

The acetyltransferase Eco1 elicits cohesin dimerization during S phaseSemantic proximity Read ↗

Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog.Semantic proximity Read ↗

Genetic evidence that the acetylation of the Smc3p subunit of cohesin modulates its ATP-bound state to promote cohesion establishment in Saccharomyces cerevisiae.Semantic proximity Read ↗

The molecular mechanism underlying Roberts syndrome involves loss of ESCO2 acetyltransferase activity.Semantic proximity Read ↗

Region-specific generation and retention of acetylated cohesin shape the genome-wide pattern of sister chromatid cohesionSemantic proximity Read ↗

Pds5 promotes and protects cohesin acetylation.Semantic proximity Read ↗

Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target.Semantic proximity Read ↗

HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle.Semantic proximity Read ↗

Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.