Protein substrates and heat shock reduce the DNA-binding ability of Escherichia coli Lon protease

1995 ◽  
Vol 44 (3-4) ◽  
pp. 484-488 ◽  
Author(s):  
S. Sonezaki ◽  
K. Okita ◽  
T. Oba ◽  
Y. Ishii ◽  
A. Kondo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Dna Binding ◽  
Lon Protease ◽  
Binding Ability ◽  
Protein Substrates

Protein substrates and heat shock reduce the DNA-binding ability of Escherichia coli Lon protease

1995 ◽  
Vol 44 (3-4) ◽  
pp. 484-488 ◽  
Author(s):  
S. Sonezaki ◽  
K. Okita ◽  
T. Oba ◽  
Y. Ishii ◽  
A. Kondo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Dna Binding ◽  
Lon Protease ◽  
Binding Ability ◽  
Protein Substrates

scholarly journals Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure.

1994 ◽  
Vol 14 (11) ◽  
pp. 7557-7568 ◽  
Author(s):  
J Zuo ◽  
R Baler ◽  
G Dahl ◽  
R Voellmy
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Heat Shock ◽  
Dna Binding ◽  
Hydrophobic Interactions ◽  
Coiled Coil ◽  
Heat Shock Transcription Factor ◽  
Single Amino Acid ◽  
Binding Ability ◽  
Heat Shock Element

Heat stress regulation of human heat shock genes is mediated by human heat shock transcription factor hHSF1, which contains three 4-3 hydrophobic repeats (LZ1 to LZ3). In unstressed human cells (37 degrees C), hHSF1 appears to be in an inactive, monomeric state that may be maintained through intramolecular interactions stabilized by transient interaction with hsp70. Heat stress (39 to 42 degrees C) disrupts these interactions, and hHSF1 homotrimerizes and acquires heat shock element DNA-binding ability. hHSF1 expressed in Xenopus oocytes also assumes a monomeric, non-DNA-binding state and is converted to a trimeric, DNA-binding form upon exposure of the oocytes to heat shock (35 to 37 degrees C in this organism). Because endogenous HSF DNA-binding activity is low and anti-hHSF1 antibody does not recognize Xenopus HSF, we employed this system for mapping regions in hHSF1 that are required for the maintenance of the monomeric state. The results of mutagenesis analyses strongly suggest that the inactive hHSF1 monomer is stabilized by hydrophobic interactions involving all three leucine zippers which may form a triple-stranded coiled coil. Trimerization may enable the DNA-binding function of hHSF1 by facilitating cooperative binding of monomeric DNA-binding domains to the heat shock element motif. This view is supported by observations that several different LexA DNA-binding domain-hHSF1 chimeras bind to a LexA-binding site in a heat-regulated fashion, that single amino acid replacements disrupting the integrity of hydrophobic repeats render these chimeras constitutively trimeric and DNA binding, and that LexA itself binds stably to DNA only as a dimer but not as a monomer in our assays.

scholarly journals Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability.

1991 ◽  
Vol 5 (10) ◽  
pp. 1902-1911 ◽  
Author(s):  
K D Sarge ◽  
V Zimarino ◽  
K Holm ◽  
C Wu ◽  
R I Morimoto
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Heat Shock Factors ◽  
Binding Ability

Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure

1994 ◽  
Vol 14 (11) ◽  
pp. 7557-7568
Author(s):  
J Zuo ◽  
R Baler ◽  
G Dahl ◽  
R Voellmy
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Heat Shock ◽  
Dna Binding ◽  
Hydrophobic Interactions ◽  
Coiled Coil ◽  
Heat Shock Transcription Factor ◽  
Single Amino Acid ◽  
Binding Ability ◽  
Heat Shock Element

Heat stress regulation of human heat shock genes is mediated by human heat shock transcription factor hHSF1, which contains three 4-3 hydrophobic repeats (LZ1 to LZ3). In unstressed human cells (37 degrees C), hHSF1 appears to be in an inactive, monomeric state that may be maintained through intramolecular interactions stabilized by transient interaction with hsp70. Heat stress (39 to 42 degrees C) disrupts these interactions, and hHSF1 homotrimerizes and acquires heat shock element DNA-binding ability. hHSF1 expressed in Xenopus oocytes also assumes a monomeric, non-DNA-binding state and is converted to a trimeric, DNA-binding form upon exposure of the oocytes to heat shock (35 to 37 degrees C in this organism). Because endogenous HSF DNA-binding activity is low and anti-hHSF1 antibody does not recognize Xenopus HSF, we employed this system for mapping regions in hHSF1 that are required for the maintenance of the monomeric state. The results of mutagenesis analyses strongly suggest that the inactive hHSF1 monomer is stabilized by hydrophobic interactions involving all three leucine zippers which may form a triple-stranded coiled coil. Trimerization may enable the DNA-binding function of hHSF1 by facilitating cooperative binding of monomeric DNA-binding domains to the heat shock element motif. This view is supported by observations that several different LexA DNA-binding domain-hHSF1 chimeras bind to a LexA-binding site in a heat-regulated fashion, that single amino acid replacements disrupting the integrity of hydrophobic repeats render these chimeras constitutively trimeric and DNA binding, and that LexA itself binds stably to DNA only as a dimer but not as a monomer in our assays.

Influence of the (1–106) fragment of Escherichia coli Lon protease on the enzyme function and DNA binding

2016 ◽  
Vol 42 (4) ◽  
pp. 381-388 ◽  
Author(s):  
A. M. Kudzhaev ◽  
E. S. Dubovtseva ◽  
O. V. Serova ◽  
A. G. Andrianova ◽  
T. V. Rotanova
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Enzyme Function ◽  
Lon Protease
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