Kyushu University, Fukuoka
SUMO-1 binding required for modification and colocalization with leukemia
Published in Lab Business Week, May 8th, 2005
"SUMO-1 is a member of a family of ubiquitin-like molecules that are post-translationally conjugated to various cellular proteins in a process that is mechanistically similar to ubiquitylation. To identify molecules that bind noncovalently to SUMO-1, we performed yeast two-hybrid screening with a SUMO-1 mutant that cannot be conjugated to target proteins as the bait. This screening resulted in the isolation of cDNAs encoding the b isoform of thymine DNA glycosylase (TDGb)," researchers in Japan reported.
"A deletion mutant of TDGb [TDGb(Delta11)]...
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Source: Lab Business Week (2005-05-08)
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