Type I ubiquitin-like proteins constitute a family of protein modifiers. Here we report the identification of a posttranslational protein modifier from Saccharomyces cerevisiae, Hub1. Overexpression of Hub1 resulted in enhanced conjugate formation when its carboxyl-terminal residue was deleted, suggesting that mature Hub1 may be produced by proteolytic processing. In vivo targets of Hub1 conjugation included cell polarity factors Sph1 and Hbt1. In the hub1Delta mutant, the subcellular localization of both Hbt1 and Sph1 was disrupted, and cell polarization during the formation of mating projections was defective. Consistent with these polarization defects, the hub1Delta mutant was deficient in mating.
机构:
Thomas Jefferson Univ, Dept Biochem & Mol Biol, Philadelphia, PA 19107 USAThomas Jefferson Univ, Dept Biochem & Mol Biol, Philadelphia, PA 19107 USA
Johnson, ES
;
Gupta, AA
论文数: 0引用数: 0
h-index: 0
机构:
Thomas Jefferson Univ, Dept Biochem & Mol Biol, Philadelphia, PA 19107 USAThomas Jefferson Univ, Dept Biochem & Mol Biol, Philadelphia, PA 19107 USA
机构:
Thomas Jefferson Univ, Dept Biochem & Mol Biol, Philadelphia, PA 19107 USAThomas Jefferson Univ, Dept Biochem & Mol Biol, Philadelphia, PA 19107 USA
Johnson, ES
;
Gupta, AA
论文数: 0引用数: 0
h-index: 0
机构:
Thomas Jefferson Univ, Dept Biochem & Mol Biol, Philadelphia, PA 19107 USAThomas Jefferson Univ, Dept Biochem & Mol Biol, Philadelphia, PA 19107 USA