J
John S. McCarty
Researcher at Heidelberg University
Publications - 16
Citations - 2078
John S. McCarty is an academic researcher from Heidelberg University. The author has contributed to research in topics: Chaperone (protein) & Heat shock protein. The author has an hindex of 15, co-authored 16 publications receiving 2015 citations. Previous affiliations of John S. McCarty include Massachusetts Institute of Technology & Institute of Molecular and Cell Biology.
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Journal ArticleDOI
The role of ATP in the functional cycle of the DnaK chaperone system
John S. McCarty,Alexander Buchberger,Alexander Buchberger,Jochen Reinstein,Bernd Bukau,Bernd Bukau +5 more
TL;DR: The rapid binding kinetics lead to the conclusion that ATP-bound DnaK is the primary form initiating interaction with substrates for chaperone activity, and the special and important role for DnaJ in stabilization of DNAK-substrate interactions is indicated.
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A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.
J. Gamer,Gerd Multhaup,Toshifumi Tomoyasu,John S. McCarty,Stefan G.D. Rüdiger,H. J. Schönfeld,C. Schirra,Hermann Bujard,Bernd Bukau +8 more
TL;DR: Data indicate that reversible inhibition of sigma32 activity through transient association of DnaK and DnaJ is a central regulatory element of the heat shock response and it is proposed that the principles of this cycle also operate in other chaperone activities of the DNAK system.
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Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication
Alexander Buchberger,Holger Theyssen,Hartwig Schröder,John S. McCarty,Giuseppe Virgallita,Philipp Milkereit,Jochen Reinstein,Bernd Bukau +7 more
TL;DR: Fluorescence analysis of the N-terminally located single tryptophan residue of DnaK revealed that the known ATP-induced alteration of the emission spectrum, proposed to result directly from conformational changes in the ATPase domain, requires the presence of the C-terminal domain and therefore mainly results from altered domain interaction.
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Antimicrobial drug discovery through bacteriophage genomics
Jing Liu,Mohammed Dehbi,Greg Moeck,Francis F. Arhin,Pascale Bauda,Dominique Bergeron,Mario Callejo,Vincent Ferretti,Nhuan Ha,Tony Kwan,John S. McCarty,Ramakrishnan Srikumar,Daniel M. Williams,Jinzi J Wu,Philippe Gros,Jerry Pelletier,Michael S. DuBow,Michael S. DuBow +17 more
TL;DR: The results suggest that mimicking the growth-inhibitory effect of phage polypeptides by a chemical compound, coupled with the plethora of phages on earth, will yield new antibiotics to combat infectious diseases.
Journal ArticleDOI
DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity.
John S. McCarty,Graham C. Walker +1 more
TL;DR: DnaK, the sole Escherichia coli member of the highly conserved 70-kDa heat shock protein (HSP70) family of proteins, autophosphorylates when incubated with ATP in vitro and it is demonstrated that threonine-199 is critical for the ATPase activity of DnaK.