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. 2005 Nov 18;337(2):517-20.
doi: 10.1016/j.bbrc.2005.09.090. Epub 2005 Sep 22.

A proline-90 residue unique to SUMO-4 prevents maturation and sumoylation

David Owerbach  1 , Eileen M McKay, Edward T H Yeh, Kenneth H Gabbay, Kurt M Bohren
Affiliations

A proline-90 residue unique to SUMO-4 prevents maturation and sumoylation

David Owerbach et al. Biochem Biophys Res Commun. .

Abstract

Four small ubiquitin-related modifier (SUMO) genes have been identified in humans. However, little is known about the basic biology of SUMO-4. Here, we report that SUMO-4 differs from SUMO-1, -2, and -3 in that the maturation process of SUMO-4 to active form containing C-terminal di-glycine residues is inhibited by a unique proline residue located at position 90 (Pro-90). Although, both the hydrolase and isopeptidase activities of SUMO peptidases are significantly diminished by Pro-90 as compared to Gln-90 (glutamine) in mutated SUMO genes, only the defective hydrolase activity appears to be biologically relevant. Native SUMO-4, thus, appears to be unable to form covalent isopeptide bonds with substrates. A biological role of SUMO-4, through non-covalent interactions is proposed.

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