High impact information on RUB1

• Our findings identify Rbx1 as a common component of enzyme systems responsible for ubiquitin and Rub1 modification of target proteins [1].
• Two genes have been identified that are required for Rub1p conjugation to Cdc53p [2].
• By analogy with Aos1p, we infer that Enr2p functions in a bipartite Rub1p-activating enzyme [2].
• Conjugation of RUB1 is not essential for normal cell growth and appears to be selective for a small set of substrates [3].
• NEDD8/Rub1 is the most homologous protein to ubiquitin among the ubiquitin-like proteins, and it is covalently linked to target proteins via the C-terminal glycine residue in a manner analogous to ubiquitylation [4].

Associations of RUB1 with chemical compounds

• An rtt101 Delta strain was hypersensitive to thiabendazole, isopropyl ( N -3-chlorophenyl) carbamate and methyl methanesulphonate, but rub1 Delta strains were not [5].
• These results suggest that this lysine residue is the site of Rub1p-dependent and -independent modifications in Rtt101p and of Rub1p-dependent modification in Cul3p [5].
• Before protein conjugation, the carboxyl-terminal asparagine residue of Rub1p is removed [6].

Other interactions of RUB1

• This suggests that Rtt101p has an additional RUB1 - and ENR2 -independent modification [5].
• Saccharomyces cerevisiae ubiquitin-like protein Rub1 conjugates to cullin proteins Rtt101 and Cul3 in vivo [5].
• The RUB1/NEDD-8 family of ubiquitin-related genes is widely represented among eukaryotes [2].
• Thus, Yuh1p is the major processing enzyme for Rub1p [6].

References