Interdomain communication in the molecular chaperone DnaK
نویسندگان
چکیده
منابع مشابه
The molecular chaperone DnaK accelerates protein evolution
Institute of Evolutionary Biology and Environmental Studies, University of Zurich, Zurich, 4 Switzerland 5 Swiss Institute of Bioinformatics, Lausanne, Switzerland 6 Department of Genetics, Smurfit Institute of Genetics, University of Dublin, Trinity College Dublin, 7 Dublin, Ireland 8 Instituto de Biología Molecular y Celular de Plantas (CSIC-UPV), Valencia, Spain 9 Department of Biology, Univ...
متن کاملThe Molecular Chaperone DnaK Is a Source of Mutational Robustness
Molecular chaperones, also known as heat-shock proteins, refold misfolded proteins and help other proteins reach their native conformation. Thanks to these abilities, some chaperones, such as the Hsp90 protein or the chaperonin GroEL, can buffer the deleterious phenotypic effects of mutations that alter protein structure and function. Hsp70 chaperones use a chaperoning mechanism different from ...
متن کاملElectrostatic Interactions between Peptides and the Molecular Chaperone DnaK
The molecular chaperone DnaK prevents intracellular protein misfolding and aggregation by transiently binding with newly synthesized polypeptides and protein folding intermediates. DnaK preferentially binds to peptides with basic residues (Arg/Lys) present on the outside of a hydrophobic core. The electrostatic contribution toward DnaK/peptide binding was determined by measuring the dissociatio...
متن کاملCrystal Structure of DnaK complexed with Nucleotide Exchange Factor GrpE in the DnaK Chaperone System: insight into the Intermolecular Communication
Background: The Hsp70 chaperone cycle mediates stress-denatured protein refolding. Results: We present the structure of a DnaK/GrpE complex containing the DnaK interdomain linker and substrate-binding domain. Conclusion: Interaction between the DnaK linker/lid regions and the GrpE N-terminal α-helix and disordered region are essential for function. Significance: The structure provides a framewo...
متن کاملMutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling.
In Escherichia coli, DnaK is essential for the replication of bacteriophage lambda DNA; this in vivo activity provides the basis of a screen for mutations affecting DnaK function. Mn PCR was used to introduce mutations into residues 405-468 of the C-terminal polypeptide-binding domain of DnaK. These mutant proteins were screened for the ability to propagate bacteriophage lambda in the backgroun...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2003
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20020943