Journal
FEBS JOURNAL
Volume 278, Issue 15, Pages 2613-2624Publisher
WILEY
DOI: 10.1111/j.1742-4658.2011.08199.x
Keywords
diphthamide; eEF1A; eEF2; eIF5A; ethanolamine phosphoglycerol; hypusine; protein modifcation; translation elongation
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Funding
- Swiss National Science Foundation [31003A-130815, 31003A-119996]
- Swiss National Science Foundation (SNF) [31003A-119996] Funding Source: Swiss National Science Foundation (SNF)
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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.
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