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Ubiquitin Signaling: Extreme Conservation as a Source of Diversity

1
Institut de Biologia Molecular de Barcelona, CSIC, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain
2
Department of Cell Biology, Harvard Medical School, Longwood, Boston, MA 02115, USA
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Author to whom correspondence should be addressed.
Cells 2014, 3(3), 690-701; https://doi.org/10.3390/cells3030690
Received: 20 March 2014 / Revised: 20 June 2014 / Accepted: 1 July 2014 / Published: 10 July 2014
(This article belongs to the Special Issue Protein Ubiquitination)
Around 2 × 103–2.5 × 103 million years ago, a unicellular organism with radically novel features, ancestor of all eukaryotes, dwelt the earth. This organism, commonly referred as the last eukaryotic common ancestor, contained in its proteome the same functionally capable ubiquitin molecule that all eukaryotic species contain today. The fact that ubiquitin protein has virtually not changed during all eukaryotic evolution contrasts with the high expansion of the ubiquitin system, constituted by hundreds of enzymes, ubiquitin-interacting proteins, protein complexes, and cofactors. Interestingly, the simplest genetic arrangement encoding a fully-equipped ubiquitin signaling system is constituted by five genes organized in an operon-like cluster, and is found in archaea. How did ubiquitin achieve the status of central element in eukaryotic physiology? We analyze here the features of the ubiquitin molecule and the network that it conforms, and propose notions to explain the complexity of the ubiquitin signaling system in eukaryotic cells. View Full-Text
Keywords: ubiquitin; proteasome; protein degradation; evolution; eukaryotes ubiquitin; proteasome; protein degradation; evolution; eukaryotes
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Zuin, A.; Isasa, M.; Crosas, B. Ubiquitin Signaling: Extreme Conservation as a Source of Diversity. Cells 2014, 3, 690-701.

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