title: Hsm3/S5b joins the ranks of 26S proteasome assembly chaperones.
abstract: In a recent issue of Molecular Cell, Le Tallec et al. (2009) characterize the yeast Hsm3 protein, an apparent ortholog of human S5b, as a dedicated chaperone that promotes assembly of the base subcomplex of the 19S proteasome activator.
authors.affiliation: Institute for Genetics, University of Cologne, Cologne, Germany.
authors.forename: Daniela
authors.initials: D
authors.lastname: Gödderz
authors.forename: R Jürgen
authors.initials: RJ
authors.lastname: Dohmen
mesh_terms: D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
chemical_list: C112193:HSM3 protein, S cerevisiae; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease