DuaJ—like蛋白研究进展

DuaJ-like蛋白由N-端保守的J区域、富含Gly和Phe区域、富含Cys区域和C-端低同源区域组成。J功能域能调节HSP70分子伴侣的ATPase活性，C-端不保守区域能调节与多肽的关系。真核细胞中存在着多种结构不同的DuaJ-like蛋白，但都含有一个J功能域。DuaJ-like蛋白通过J功能域调节HSP70功能而参与蛋白的折叠、装配和运输过程。

Advance in DuaJ-like protein

DuaJ-like proteins possess four domain:an N-terminal J domain, a adjacent domainthat is rich in glycine and phenylalanine residues, a central domain containing four repeats of aCXXCXGXG motif and a less well-conserved C-terminal domain. Members of the DuaJ-like protein family are structurally diverse,containing different combinations of three conserved domains.A11 DuaJ-like proteins contain a J-domain,which is proposed to mediate interactions with HSP70that regulate ATPase activity.The C-terminal domain that is thought to be involved in proteinsubstrate binding. DuaJ-like proteins participate in complex biological processes,such as proteinfolding, translocation and the assembly of transient complex structures.