scholarly journals Isolation and Identification of Putative Protein Substrates of the AAA+ Molecular Chaperone ClpB from the Pathogenic Spirochaete Leptospira interrogans

2018 ◽  
Vol 19 (4) ◽  
pp. 1234 ◽  
Author(s):  
Joanna Krajewska ◽  
Zbigniew Arent ◽  
Michal Zolkiewski ◽  
Sabina Kędzierska-Mieszkowska
Keyword(s):  
Molecular Chaperone ◽  
Leptospira Interrogans ◽  
Isolation And Identification ◽  
Protein Substrates ◽  
Putative Protein

Synthetic and biological approaches to map substrate specificities of proteases

2019 ◽  
Vol 401 (1) ◽  
pp. 165-182 ◽  
Author(s):  
Shiyu Chen ◽  
Joshua J. Yim ◽  
Matthew Bogyo
Keyword(s):  
Substrate Specificity ◽  
Antigen Processing ◽  
Therapeutic Agents ◽  
Protein Catabolism ◽  
Parasite Invasion ◽  
Peptide Substrates ◽  
Protein Substrates ◽  
Putative Protein ◽  
Natural Protein ◽  
Biological Methods

Abstract Proteases are regulators of diverse biological pathways including protein catabolism, antigen processing and inflammation, as well as various disease conditions, such as malignant metastasis, viral infection and parasite invasion. The identification of substrates of a given protease is essential to understand its function and this information can also aid in the design of specific inhibitors and active site probes. However, the diversity of putative protein and peptide substrates makes connecting a protease to its downstream substrates technically difficult and time-consuming. To address this challenge in protease research, a range of methods have been developed to identify natural protein substrates as well as map the overall substrate specificity patterns of proteases. In this review, we highlight recent examples of both synthetic and biological methods that are being used to define the substrate specificity of protease so that new protease-specific tools and therapeutic agents can be developed.

A molecular chaperone complex at the lysosomal membrane is required for protein translocation

2001 ◽  
Vol 114 (13) ◽  
pp. 2491-2499 ◽  
Author(s):  
Fernando A. Agarraberes ◽  
J. Fred Dice
Keyword(s):  
Molecular Chaperone ◽  
Hip Hop ◽  
Protein Translocation ◽  
Lysosomal Membrane ◽  
Interacting Protein ◽  
Protein Substrates ◽  
Proteolytic Pathway ◽  
Cytosolic Side ◽  
Chaperone Complex ◽  
Chaperone Mediated Autophagy

A group of cytosolic proteins are targeted to lysosomes for degradation in response to serum withdrawal or prolonged starvation by a process termed chaperone-mediated autophagy. In this proteolytic pathway little is known about how proteins are translocated across lysosomal membranes. We now show that an isoform of the constitutively expressed protein of the heat shock family of 70 kDa (Hsc70) is associated with the cytosolic side of the lysosomal membrane where it binds to substrates of this proteolytic pathway. Results from coimmunoprecipitation and colocalization studies indicate that this molecular chaperone forms complexes with other molecular chaperones and cochaperones, including Hsp90, Hsp40, the Hsp70-Hsp90 organizing protein (Hop), the Hsp70-interacting protein (Hip), and the Bcl2-associated athanogene 1 protein (BAG-1). Antibodies against Hip, Hop, Hsp40 and Hsc70 block transport of protein substrates into purified lysosomes.

The Isolation and Identification of Leptospira interrogans Serovar Bratislava from a Pig in Germany*

1992 ◽  
Vol 39 (1-10) ◽  
pp. 362-368 ◽  
Author(s):  
A. Schönberg ◽  
Bärbel Hahn-Hey ◽  
Ulrike Kämpe ◽  
Katrin Schmidt ◽  
W. A. Ellis
Keyword(s):  
Leptospira Interrogans ◽  
Isolation And Identification

scholarly journals Thermodynamic Analysis of a Molecular Chaperone Binding to Unfolded Protein Substrates

Biochemistry ◽  
2010 ◽  
Vol 49 (6) ◽  
pp. 1346-1353 ◽  
Author(s):  
Ying Xu ◽  
Sebastian Schmitt ◽  
Liangjie Tang ◽  
Ursula Jakob ◽  
Michael C. Fitzgerald
Keyword(s):  
Thermodynamic Analysis ◽  
Molecular Chaperone ◽  
Protein Substrates ◽  
Unfolded Protein ◽  
Chaperone Binding

scholarly journals Characterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans

PLoS ONE ◽  
2017 ◽  
Vol 12 (7) ◽  
pp. e0181118 ◽  
Author(s):  
Joanna Krajewska ◽  
Anna Modrak-Wójcik ◽  
Zbigniew J. Arent ◽  
Daniel Więckowski ◽  
Michal Zolkiewski ◽  
...  
Keyword(s):  
Molecular Chaperone ◽  
Leptospira Interrogans

scholarly journals ATP-driven Non-equilibrium Activation of Kinase Clients by the Molecular Chaperone Hsp90

2020 ◽  
Author(s):  
Huafeng Xu
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperone ◽  
Late Stage ◽  
Active Conformation ◽  
Cell Type ◽  
Protein Activation ◽  
Protein Substrates ◽  
Cell Type Specific ◽  
Kinetics Of

AbstractThe molecular chaperone 90-kDa heat-shock protein (Hsp90) assists the late-stage folding and activation of diverse types of protein substrates (called clients), including many kinases. Previous studies have established that the Hsp90 homodimer undergoes an ATP-driven cycle through open and closed conformations. Here I propose a model of client activation by Hsp90, which predicts that this cycle enables Hsp90 to use ATP energy to drive a client out of thermodynamic equilibrium toward its active conformation. My model assumes that an Hsp90-bound client can transition between a deactivating conformation and an activating conformation. It suggests that the cochaperone Cdc37 aids Hsp90 to activate kinase clients by differentiating between these two intermediate conformations. My model makes experimentally testable predictions, including how modulating the stepwise kinetics of the Hsp90 cycle—for example, by various cochaperones—affects the activation of different clients. My model may inform client-specific and cell-type-specific therapeutic intervention of Hsp90-mediated protein activation.

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