Disease relevance of URM1

• Non-covalent interaction between nucleocapsid protein of Tula hantavirus and small ubiquitin-related modifier-1, SUMO-1 [1].

High impact information on URM1

• We report here that Zip3 is a SUMO (small ubiquitin-related modifier) E3 ligase and that Zip1 is a binding protein for SUMO-conjugated products [2].
• The ubiquitin-like protein SUMO-1 (small ubiquitin-related modifier 1) is covalently attached to substrate proteins by ligases and cleaved by isopeptidases [3].
• Small ubiquitin-related modifier pathway is a major determinant of doxorubicin cytotoxicity in Saccharomyces cerevisiae [4].
• We report that Ste12 and Tec1 undergo covalent modification by the ubiquitin-related modifier SUMO [5].
• Here we report that tah mutant ubc9-10 harbors a hypomorphic allele of UBC9, which encodes the essential SUMO (small ubiquitin-related modifier) E2-conjugating enzyme [6].

Biological context of URM1

• Like ubiquitylation, protein modification with the small ubiquitin-related modifier SUMO appears to be important during mitosis, because yeast cells impaired in the SUMO-conjugating enzyme Ubc9 were found to be blocked in mitosis and defective in cyclin degradation [7].
• Urm1p is a ubiquitin-related protein that serves as a posttranslational modification of other proteins [8].
• Defects in SUMO (small ubiquitin-related modifier) conjugation and deconjugation alter cell sensitivity to DNA topoisomerase I-induced DNA damage [6].

Associations of URM1 with chemical compounds

• Urm1 is conjugated to target proteins, which requires the C-terminal glycine of Urm1 [9].
• Urm1 and Uba4 show similarity to prokaryotic proteins essential for molybdopterin and thiamin biosynthesis, although the Urm1 system is not involved in these pathways [9].
• SUMO (small ubiquitin-related modifier) modulates protein structure and function by covalently binding to the lysine side chains of the target proteins [10].

Other interactions of URM1

• At the first step of this reaction, Urm1 forms a thioester with a novel E1-like protein, Uba4 [9].
• Simultaneous loss of Urm1p and Cla4p, a p21-activated kinase that functions in budding, is lethal [11].
• Moreover, treatment of cells with thiol-specific oxidants affects the abundance of Ahp1p-Urm1p conjugates [8].
• In S phase, even in the absence of exogenous DNA damage, yeast PCNA can be alternatively modified by the small ubiquitin-related modifier protein SUMO; however the consequences of this remain controversial [12].

References