Abstract
In Escherichia coli, the DnaK/DnaJ chaperone can control the stability and activity of σ32, 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 σ32 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 σ32 and DnaK to increase the level of HSPs, such as GroEL, DnaK, and σ32. These results suggested that the zinc finger domain was conserved during evolution.
MeSH terms
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Arabidopsis / chemistry
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Arabidopsis / enzymology*
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Arabidopsis / genetics
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Arabidopsis Proteins / chemistry
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Arabidopsis Proteins / genetics
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Arabidopsis Proteins / metabolism*
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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HSP40 Heat-Shock Proteins / genetics
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HSP40 Heat-Shock Proteins / metabolism*
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HSP70 Heat-Shock Proteins / genetics
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HSP70 Heat-Shock Proteins / metabolism*
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Heat-Shock Proteins / genetics
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Heat-Shock Proteins / metabolism*
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism*
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Protein Binding
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Protein Domains
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Sigma Factor / genetics
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Sigma Factor / metabolism*
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Ubiquitin-Protein Ligases / chemistry
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Ubiquitin-Protein Ligases / genetics
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Ubiquitin-Protein Ligases / metabolism*
Substances
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Arabidopsis Proteins
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DnaJ protein, E coli
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Escherichia coli Proteins
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HSP40 Heat-Shock Proteins
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HSP70 Heat-Shock Proteins
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Heat-Shock Proteins
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Molecular Chaperones
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Sigma Factor
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heat-shock sigma factor 32
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NLA protein, Arabidopsis
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Ubiquitin-Protein Ligases
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dnaK protein, E coli