A gram-negative characteristic segment in Escherichia coli DnaK is essential for the ATP-dependent cooperative function with the co-chaperones DnaJ and GrpE

Autor: Chihana Higashi, Jiro Nakayama, Kenji Sonomoto, Kozue Saruwatari, Shinya Sugimoto
Rok vydání: 2007
Předmět:
Gram-negative bacteria
ATPase
Mutant
Molecular Sequence Data
Biophysics
lac operon
medicine.disease_cause
Biochemistry
DnaJ
DnaK
Evolution
Molecular
Adenosine Triphosphate
Structural Biology
Protein-fragment complementation assay
Heat shock protein
Gram-Negative Bacteria
Genetics
medicine
Escherichia coli
HSP70 Heat-Shock Proteins
Amino Acid Sequence
Protein Structure
Quaternary
GrpE
Molecular Biology
Heat-Shock Proteins
Adenosine Triphosphatases
biology
Sequence Homology
Amino Acid
Circular Dichroism
Escherichia coli Proteins
Genetic Complementation Test
Cell Biology
HSP40 Heat-Shock Proteins
biology.organism_classification
Protein Structure
Tertiary
Cooperation
Chaperone (protein)
Molecular chaperone
biology.protein
Gram-negative and -positive bacteria
bacteria
Mutant Proteins
Gene Deletion
Molecular Chaperones
Protein Binding
Zdroj: FEBS letters. 581(16)
ISSN: 0014-5793
Popis: We describe importance of the characteristic segment in ATPase domain of DnaK chaperone which is present in all gram-negative bacteria but is absent in all gram-positive bacteria. In vitro studies, ATPase activity, luciferase-refolding activity, and surface plasmon resonance analyses, demonstrated that a segment-deletion mutant DnaKDelta74-96 became defective in the cooperation with the co-chaperones DnaJ and GrpE. In addition, in vivo complementation assay showed that expression of DnaKDelta74-96 could not rescue the viability of Escherichia coli DeltadnaK mutant at 43 degrees C. Consequently, we suggest evolutionary significance for this DnaK ATPase domain segment in gram-negative bacteria towards the DnaK chaperone system.
Databáze: OpenAIRE
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