Principal Investigator Frank Solomon
Rbl2p binds beta-tubulin to form a heterodimer. Although dispensable for mitotic growth under normal conditions, it is essential in strains with beta-tubulin in even modest excess, such as tub3D. The lethality of overexpressed beta-tubulin is suppressed by overexpressed Rbl2p. Suppression occurs at Rbl2p levels substantially substoichiometric to the undimerized beta-tubulin. Rbl2p may act as a chaperone, transiently binding to beta-tubulin to restrict its interactions until it aggregates and is no longer toxic.