Format

Send to

Choose Destination
Sci Rep. 2016 Feb 10;6:21304. doi: 10.1038/srep21304.

Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms.

Author information

1
Department of Biomedical Sciences and Medicine, Faro, Portugal.
2
Center for Biomedical Research (CBMR), Faro, Portugal.
3
ProRegeM-PhD Program in Mechanisms of Disease and Regenerative Medicine, Faro, Portugal.
4
Instituto Gulbenkian de Ciência, Rua da Quinta Grande 6, Oeiras 2781-901, Portugal.
5
Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium.
6
Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium.
7
Center of Marine Sciences, University of Algarve, Faro, Portugal.

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.

PMID:
26861501
PMCID:
PMC4748286
DOI:
10.1038/srep21304
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center