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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Owerbach D,McKay EM,Yeh ET,Gabbay KH,Bohren KMdoi
10.1016/j.bbrc.2005.09.090subject
Has Abstractpub_date
2005-11-18 00:00:00pages
517-20issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(05)02116-9journal_volume
337pub_type
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