ArticleStructure (London, England : 1993)2019
Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex.
Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 58 citations in OpenAlex.
- Mechanisms of Congenital Heart Disease Caused by NAA15 Haploinsufficiency.Circulation research · 2021Trial
- NatA engages in multi-factor complexes at the ribosomal polypeptide tunnel exit.Nature communications · 2026Article
- Article
- Natural History of NAA15 -Related Neurodevelopmental Disorder Through Adolescence.American journal of medical genetics. Part A · 2025Article
- Illuminating the impact of N-terminal acetylation: from protein to physiology.Nature communications · 2025Review
- Purification and activity assays of N-terminal acetyltransferase D.Methods in enzymology · 2025Article
- Conformational plasticity links structural instability of NAA10Computational and structural biotechnology journal · 2024Article
- Multi-protein assemblies orchestrate co-translational enzymatic processing on the human ribosome.Nature communications · 2024Article
- Diverging co-translational protein complex assembly pathways are governed by interface energy distribution.Nature communications · 2024Article
- Acetyltransferase in cardiovascular disease and aging.The journal of cardiovascular aging · 2024Article
- Molecular role of NAA38 in thermostability and catalytic activity of the human NatC N-terminal acetyltransferase.Structure (London, England : 1993) · 2023Article
- Extended N-Terminal Acetyltransferase Naa50 in Filamentous Fungi Adds to Naa50 Diversity.International journal of molecular sciences · 2022Article
- Pan-cancer analysis reveals NAA50 as a cancer prognosis and immune infiltration-related biomarker.Frontiers in genetics · 2022Article
- Molecular mechanism of N-terminal acetylation by the ternary NatC complex.Structure (London, England : 1993) · 2021Article
- Charting the N-Terminal Acetylome: A Comprehensive Map of Human NatA Substrates.International journal of molecular sciences · 2021Article
- Novel Bisubstrate Inhibitors for Protein N-Terminal Acetyltransferase D.Journal of medicinal chemistry · 2021Article
- Harnessing Ionic Selectivity in Acetyltransferase Chemoproteomic Probes.ACS chemical biology · 2021Article
- Structural basis of Naa20 activity towards a canonical NatB substrate.Communications biology · 2021Article
- Cornelia de Lange Syndrome as Paradigm of Chromatinopathies.Frontiers in neuroscience · 2021Review
- Variants in NAA15 cause pediatric hypertrophic cardiomyopathy.American journal of medical genetics. Part A · 2021Article
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6 authors at 3 institutions in 1 country.
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Abstract
NatA co-translationally acetylates the N termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). The molecular basis of association between Naa50 and NatA and the mechanism for how their association affects their catalytic activities in yeast and human are poorly understood. Here, we determined the X-ray crystal structure of yeast NatA/Naa50 as a scaffold to understand coregulation of NatA/Naa50 activity in both yeast and human. We find that Naa50 makes evolutionarily conserved contacts to both the Naa10 and Naa15 subunits of NatA. These interactions promote catalytic crosstalk within the human complex, but do so to a lesser extent in the yeast complex, where Naa50 activity is compromised. These studies have implications for understanding the role of the NatA/Naa50 complex in modulating the majority of the N-terminal acetylome in diverse species.
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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.