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Article
The EMBO Journal (2000) 19, 5916–5929, doi:10.1093/emboj/19.21.5916
Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
Carmela Giglione, Alexandre Serero, Michèle Pierre, Bertrand Boisson and Thierry Meinnel
Institut des Sciences Végétales, UPR40, Centre National de la Recherche Scientifique, Bâtiment 23, 1 avenue de la Terrasse, F-91198 Gif-sur-Yvette Cedex, France

To whom correspondence should be addressed
Thierry Meinnel, meinnel@isv.cnrs-gif.fr

Received 7 August 2000; Revised 13 September 2000; Accepted 13 September 2000.
Abstract
The N-terminal protein processing pathway is an essential mechanism found in all organisms. However, it is widely believed that deformylase, a key enzyme involved in this process in bacteria, does not exist in eukaryotes, thus making it a target for antibacterial agents such as actinonin. In an attempt to define this process in higher eukaryotes we have used Arabidopsis thaliana as a model organism. Two deformylase cDNAs, the first identified in any eukaryotic system, and six distinct methionine aminopeptidase cDNAs were cloned. The corresponding proteins were characterized in vivo and in vitro. Methionine aminopeptidases were found in the cytoplasm and in the organelles, while deformylases were localized in the organelles only. Our work shows that higher plants have a much more complex machinery for methionine removal than previously suspected. We were also able to identify deformylase homologues from several animals and clone the corresponding cDNA from human cells. Our data provide the first evidence that lower and higher eukaryotes, as well as bacteria, share a similar N-terminal protein processing machinery, indicating universality of this system.
Keywords: Arabidopsis thaliana, homologues, methionine removal, peptide deformylase, protein processing
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