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DuaJ—like蛋白研究进展
Advance in DuaJ-like protein
【摘要】 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。
【Abstract】 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.
【Key words】 DuaJ-like protein; molecular chaperone; structure; function;
- 【文献出处】 生命科学 ,CHINESE BULLETIN OF LIFE SCIENCES , 编辑部邮箱 ,1999年04期
- 【被引频次】3
- 【下载频次】62