BAH1 an E3 Ligase from Arabidopsis Thaliana Stabilizes Heat Shock Factor σ of Escherichia Coli by Interacting with DnaK/DnaJ Chaperone Team

Overview

Journal Curr Microbiol

Specialty Microbiology

Date 2017 Dec 21

PMID 29260303

Citations 3

Authors

Xibing Xu

Ke Liang

Yulong Niu

Yan Shen

Xuedong Wan

Haiyan Li

Yi Yang

Affiliations

Soon will be listed here.

Abstract

In Escherichia coli, the DnaK/DnaJ chaperone can control the stability and activity of σ, which is the key factor in heat shock response. Heterologous expression of eukaryotic molecular chaperones protects E. coli from heat stress. Here, we show that BAH1, an E3 ligase from plant that has a similar zinc finger domain to DnaJ, can perform block the effect of DnaK on σ in Escherichia coli. By constructing a chimeric DnaJ protein, with the J-domain of DnaJ fused to BAH1, we found BAH1 could partially compensate for the DnaJ' zinc finger domain in vivo, and that it was dependent on the zinc finger domain of BAH1. Furthermore, BAH1 could interact with both σ and DnaK to increase the level of HSPs, such as GroEL, DnaK, and σ. These results suggested that the zinc finger domain was conserved during evolution.

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