Evolution and function of ubiquitin-like protein-conjugation systems.
Ubiquitin functions by covalently modifying other proteins. In the past few years, a surprising number of other proteins have been identified that, despite often being only slightly similar to ubiquitin, can also be attached to proteins. Newly discovered parallels between the activation of ubiquitin and the biosynthesis of certain enzyme cofactors now hint at the possible evolutionary origins of the ubiquitin system.
Department of Molecular Biophysics & Biochemistry, Yale University, 266 Whitney Avenue, New Haven, Connecticut 06520, USA. mark.hochstrasser@yale.edu
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D000595:Amino Acid Sequence; D000818:Animals; D003067:Coenzymes / Q000378:metabolism; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D011506:Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D016415:Sequence Alignment; D015398:Signal Transduction; D014452:Ubiquitins / Q000737:chemistry* / Q000378:metabolism*
D003067:Coenzymes; D011506:Proteins; D014452:Ubiquitins