Signorell, Aita; Jelk, Jennifer; Rauch, Monika; Bütikofer, Peter (2008). Phosphatidylethanolamine is the precursor of the ethanolamine phosphoglycerol moiety bound to eukaryotic elongation factor 1A. Journal of biological chemistry, 283(29), pp. 20320-9. Bethesda, Md.: American Society for Biochemistry and Molecular Biology 10.1074/jbc.M802430200
Full text not available from this repository.In addition to its conventional role during protein synthesis, eukaryotic elongation factor 1A is involved in other cellular processes. Several regions of interaction between eukaryotic elongation factor 1A and the translational apparatus or the cytoskeleton have been identified, yet the roles of the different post-translational modifications of eukaryotic elongation factor 1A are completely unknown. One amino acid modification, which so far has only been found in eukaryotic elongation factor 1A, consists of ethanolamine-phosphoglycerol attached to two glutamate residues that are conserved between mammals and plants. We now report that ethanolamine-phosphoglycerol is also present in eukaryotic elongation factor 1A of the protozoan parasite Trypanosoma brucei, indicating that this unique protein modification is of ancient origin. In addition, using RNA-mediated gene silencing against enzymes of the Kennedy pathway, we demonstrate that phosphatidylethanolamine is a direct precursor of the ethanolamine-phosphoglycerol moiety. Down-regulation of the expression of ethanolamine kinase and ethanolamine-phosphate cytidylyltransferase results in inhibition of phosphatidylethanolamine synthesis in T. brucei procyclic forms and, concomitantly, in a block in glycosylphosphatidylinositol attachment to procyclins and ethanolamine-phosphoglycerol modification of eukaryotic elongation factor 1A.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine |
UniBE Contributor: |
Bütikofer, Peter |
ISSN: |
0021-9258 |
ISBN: |
18499667 |
Publisher: |
American Society for Biochemistry and Molecular Biology |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 15:03 |
Last Modified: |
05 Dec 2022 14:19 |
Publisher DOI: |
10.1074/jbc.M802430200 |
PubMed ID: |
18499667 |
Web of Science ID: |
000257565300048 |
URI: |
https://boris.unibe.ch/id/eprint/27320 (FactScience: 106024) |
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