Unique modifications of translation elongation factors

Greganova, Eva; Altmann, Michael; Bütikofer, Peter (2011). Unique modifications of translation elongation factors. FEBS journal, 278(15), pp. 2613-24. Oxford: Wiley-Blackwell 10.1111/j.1742-4658.2011.08199.x

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Covalent modifications of proteins often modulate their biological functions or change their subcellular location. Among the many known protein modifications, three are exceptional in that they only occur on single proteins: ethanolamine phosphoglycerol, diphthamide and hypusine. Remarkably, the corresponding proteins carrying these modifications, elongation factor 1A, elongation factor 2 and initiation factor 5A, are all involved in elongation steps of translation. For diphthamide and, in part, hypusine, functional essentiality has been demonstrated, whereas no functional role has been reported so far for ethanolamine phosphoglycerol. We review the biosynthesis, attachment and physiological roles of these unique protein modifications and discuss common and separate features of the target proteins, which represent essential proteins in all organisms.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Altmann, Michael and Bütikofer, Peter

ISSN:

1742-464X

Publisher:

Wiley-Blackwell

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:23

Last Modified:

06 Dec 2013 13:29

Publisher DOI:

10.1111/j.1742-4658.2011.08199.x

PubMed ID:

21624055

Web of Science ID:

000292933300001

URI:

https://boris.unibe.ch/id/eprint/8142 (FactScience: 213629)

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