ArticleThe Journal of biological chemistry2016
Human Naa50 Protein Displays Broad Substrate Specificity for Amino-terminal Acetylation: DETAILED STRUCTURAL AND BIOCHEMICAL ANALYSIS USING TETRAPEPTIDE LIBRARY.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Deciphering the Molecular Basis of Systemic Manifestations in Cutaneous Leishmaniasis Using Integrated Bioinformatics Analysis.Acta parasitologica · 2026Article
- Orbitofrontal intronic circular RNA from Nrxn3 mediates reward learning and motivation for reward.Progress in neurobiology · 2024Article
- Highly pathogenic natural monoclonal antibody B4-IgM recognizes a post-translational modification comprised of acetylated N-terminal methionine followed by aspartic or glutamic acid.Molecular immunology · 2023Article
- Human Naa50 Shows SerotoninAntioxidants (Basel, Switzerland) · 2023Article
- Extended N-Terminal Acetyltransferase Naa50 in Filamentous Fungi Adds to Naa50 Diversity.International journal of molecular sciences · 2022Article
- Human exposure to low dose ionizing radiation affects miR-21 and miR-625 expression levels.Molecular biology reports · 2022Article
- Cornelia de Lange Syndrome as Paradigm of Chromatinopathies.Frontiers in neuroscience · 2021Review
- NAA50 Is an Enzymatically ActivePlant physiology · 2020Article
- Loss of the Acetyltransferase NAA50 Induces Endoplasmic Reticulum Stress and Immune Responses and Suppresses Growth.Plant physiology · 2020Article
- Structural basis of HypK regulating N-terminal acetylation by the NatA complex.Nature communications · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amino-terminal acetylation is a critical co-translational modification of the newly synthesized proteins in a eukaryotic cell carried out by six amino-terminal acetyltransferases (NATs). All NATs contain at least one catalytic subunit, and some contain one or two additional auxiliary subunits. For example, NatE is a complex of Naa10, Naa50, and Naa15 (auxiliary). In the present study, the crystal structure of human Naa50 suggested the presence of CoA and acetylated tetrapeptide (AcMMXX) that have co-purified with the protein. Biochemical and thermal stability studies on the tetrapeptide library with variations in the first and second positions confirm our results from the crystal structure that a peptide with Met-Met in the first two positions is the best substrate for this enzyme. In addition, Naa50 acetylated all MXAA peptides except for MPAA. Transcriptome analysis of 10 genes that make up six NATs in humans from eight different cell lines suggests that components of NatE are transcribed in all cell lines, whereas others are variable. Because Naa10 is reported to acetylate all amino termini that are devoid of methionine and Naa50 acetylates all other peptides that are followed by methionine, we believe that NatE complex can be a major contributor for amino-terminal acetylation at the ribosome exit tunnel.
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