11 research outputs found
Estrutura e propriedades do aço inoxidável austenÃtico AISI 316L Grau ASTM F138 nitretado sob plasma à baixa temperatura
Low temperature plasma carburizing of AISI 316L austenitic stainless steel and AISI F51 duplex stainless steel
Poisson Effects on X-Ray Diffraction Patterns in Low-Temperature-Carburized Austenitic Stainless Steel
Effects of the Process Parameters on the Microstructure and Properties of Nitrided 17-4PH Stainless Steel
Overexpression of Yeast Hsp110 Homolog Sse1p Suppresses ydj1-151 Thermosensitivity and Restores Hsp90-dependent Activity
The Saccharomyces cerevisiae heat-shock protein (Hsp)40, Ydj1p, is involved in a variety of cellular activities that control polypeptide fate, such as folding and translocation across intracellular membranes. To elucidate the mechanism of Ydj1p action, and to identify functional partners, we screened for multicopy suppressors of the temperature-sensitive ydj1-151 mutant and identified a yeast Hsp110, SSE1. Overexpression of Sse1p also suppressed the folding defect of v-Src kinase in the ydj1-151 mutant and partially reversed the α-factor translocation defect. SSE1-dependent suppression of ydj1-151 thermosensitivity required the wild-type ATP-binding domain of Sse1p. However, the Sse1p mutants maintained heat-denatured firefly luciferase in a folding-competent state in vitro and restored human androgen receptor folding in sse1 mutant cells. Because the folding of both v-Src kinase and human androgen receptor in yeast requires the Hsp90 complex, these data suggest that Ydj1p and Sse1p are interacting cochaperones in the Hsp90 complex and facilitate Hsp90-dependent activity