The molecular chaperone TF55
نویسندگان
چکیده
منابع مشابه
Conformational dynamics of the molecular chaperone Hsp90.
The ubiquitous molecular chaperone Hsp90 makes up 1-2% of cytosolic proteins and is required for viability in eukaryotes. Hsp90 affects the folding and activation of a wide variety of substrate proteins including many involved in signaling and regulatory processes. Some of these substrates are implicated in cancer and other diseases, making Hsp90 an attractive drug target. Structural analyses h...
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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...
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This review is focused on the mechanisms by which ATP binding and hydrolysis drive chaperone machines assisting protein folding and unfolding. A survey of the key, general chaperone systems Hsp70 and Hsp90, and the unfoldase Hsp100 is followed by a focus on the Hsp60 chaperonin machine which is understood in most detail. Cryo-electron microscopy analysis of the E. coli Hsp60 GroEL reveals inter...
متن کاملEditorial: The HSP70 Molecular Chaperone Machines
The HSP70s belong to a small family of highly conserved ∼70 kDa enzymes that can use the energy of ATP-hydrolysis to modify the structure, and consequently the function, of specific native proteins, and to unfold, solubilize, and thereby reduce the cellular concentration of harmful misfolded proteins (Finka et al., 2016). Particular HSP70s are expressed constitutively in the cytosol of bacteria...
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Background: The chaperone activity of Mycobacterium tuberculosis Acr is an important function that helps to prevent misfolding of protein substrates inside the host, especially in conditions of hypoxia. Objectives: The aim of this study was to establish the correlation of structure and function of recombinant Acr proteins both before and after ge...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1994
ISSN: 0014-5793
DOI: 10.1016/0014-5793(94)80447-8