期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 285, 期 44, 页码 34231-34239出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.144642
关键词
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资金
- Ministerio de Educacion e Innovacion [BFU2007-64452]
- Gobierno Vasco [IT-358-07]
- Diputacion Foral de Bizkaia [DIPE08/18]
DnaJ from Escherichia coli is a Type I Hsp40 that functions as a cochaperone of DnaK(Hsp70), stimulating its ATPase activity and delivering protein substrates. How DnaJ binds protein substrates is still poorly understood. Here we have studied the role of DnaJ G/F-rich domain in binding of several substrates with different conformational properties (folded, partially (un) folded and unfolded). Using partial proteolysis we find that RepE, a folded substrate, contacts a wide DnaJ area that involves part of the G/F-rich region and Zn-binding domain. Deletion of G/F-rich region hampers binding of native RepE and reduced the affinity for partially (un) folded substrates. However, binding of completely unfolded substrates is independent on the G/F-rich region. These data indicate that DnaJ distinguishes the substrate conformation and is able to adapt the use of the G/F-rich region to form stable substrate complexes.
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