Format:
Online-Ressource
ISSN:
1460-2075
Content:
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.
In:
volume:19
In:
number:21
In:
year:2000
In:
pages:5916-5929
In:
extent:14
In:
European Molecular Biology Organization, The EMBO journal, Heidelberg : EMBO Press, 1982-, 19, Heft 21 (2000), 5916-5929 (gesamt 14), 1460-2075
Language:
English
DOI:
10.1093/emboj/19.21.5916
URN:
urn:nbn:de:101:1-2023110406274310699691
URL:
https://doi.org/10.1093/emboj/19.21.5916
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2023110406274310699691
URL:
https://d-nb.info/1308573146/34
URL:
https://doi.org/10.1093/emboj/19.21.5916
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