Cyr D M
Institut für Physiologische Chemie der Universität München, Germany.
FEBS Lett. 1995 Feb 13;359(2-3):129-32. doi: 10.1016/0014-5793(95)00024-4.
Ydj1p, a cytosolic DnaJ homolog from Saccharomyces cerevisiae, is demonstrated to function as a molecular chaperone. Purified Ydj1p formed complexes with non-native polypeptides and suppressed protein aggregation. Ydj1p cooperated with Ssa Hsp70 proteins in the prevention of protein aggregation, but not with the Ssb Hsp70 proteins. Cooperation between these different molecular chaperones was only observed in the presence of hydrolyzable ATP and correlated with the ability of Ydj1p to stimulate the ATPase activity of the Hsp70 homolog with which it was paired. The regulatory and chaperone activities of a eukarytic DnaJ homolog thus act together to assist Hsp70 in modulating the conformation of proteins.
Ydj1p是一种来自酿酒酵母的胞质DnaJ同源物，已被证明具有分子伴侣功能。纯化的Ydj1p与非天然多肽形成复合物并抑制蛋白质聚集。Ydj1p与Ssa Hsp70蛋白协同作用以防止蛋白质聚集，但不与Ssb Hsp70蛋白协同作用。这些不同分子伴侣之间的协同作用仅在存在可水解ATP的情况下观察到，并且与Ydj1p刺激与其配对的Hsp70同源物的ATPase活性的能力相关。因此，真核生物DnaJ同源物的调节和伴侣活性共同作用，以协助Hsp70调节蛋白质的构象。
