title: Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms.
abstract: Protein N-terminal acetylation is an ancient and ubiquitous co-translational modification catalyzed by a highly conserved family of N-terminal acetyltransferases (NATs). Prokaryotes have at least 3 NATs, whereas humans have six distinct but highly conserved NATs, suggesting an increase in regulatory complexity of this modification during eukaryotic evolution. Despite this, and against our initial expectations, we determined that NAT diversification did not occur in the eukaryotes, as all six major human NATs were most likely present in the Last Eukaryotic Common Ancestor (LECA). Furthermore, we also observed that some NATs were actually secondarily lost during evolution of major eukaryotic lineages; therefore, the increased complexity of the higher eukaryotic proteome occurred without a concomitant diversification of NAT complexes.
authors: Department of Biomedical Sciences and Medicine, Faro, Portugal.|Center for Biomedical Research (CBMR), Faro, Portugal.|ProRegeM-PhD Program in Mechanisms of Disease and Regenerative Medicine, Faro, Portugal.
authors: Om Singh
authors: OS
authors: Rathore
authors: Department of Biomedical Sciences and Medicine, Faro, Portugal.|Center for Biomedical Research (CBMR), Faro, Portugal.
authors: Alexandra
authors: A
authors: Faustino
authors: Department of Biomedical Sciences and Medicine, Faro, Portugal.|Center for Biomedical Research (CBMR), Faro, Portugal.|Instituto Gulbenkian de Ciência, Rua da Quinta Grande 6, Oeiras 2781-901, Portugal.
authors: Pedro
authors: P
authors: Prudêncio
authors: Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium.|Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium.
authors: Petra
authors: P
authors: Van Damme
authors: Center of Marine Sciences, University of Algarve, Faro, Portugal.
authors: Cymon J
authors: CJ
authors: Cox
authors: Department of Biomedical Sciences and Medicine, Faro, Portugal.|Center for Biomedical Research (CBMR), Faro, Portugal.|Instituto Gulbenkian de Ciência, Rua da Quinta Grande 6, Oeiras 2781-901, Portugal.
authors: Rui Gonçalo
authors: RG
authors: Martinho
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D017360:Arabidopsis / Q000201:enzymology* / Q000378:metabolism; D005075:Biological Evolution; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000378:metabolism; D005057:Eukaryotic Cells / Q000201:enzymology* / Q000378:metabolism; D014644:Genetic Variation; D006801:Humans; D063206:N-Terminal Acetyltransferases / Q000235:genetics*; D020543:Proteome / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D020543:Proteome; D063206:N-Terminal Acetyltransferases