The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis
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چکیده
منابع مشابه
The 90-kDa heat shock protein (hsp-90) possesses an ATP binding site and autophosphorylating activity.
The 90-kDa heat shock protein (hsp-90) is an abundant cytosolic protein believed to play a role in maintenance of protein trafficking and closely associated with several steroid hormone receptors. Incubation of highly purified hsp-90 with [gamma-32P]ATP results in its autophosphorylation on serine residues. There are several lines of evidence which suggest that this activity is due to a kinase ...
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Toxoplasmosis is a common and widespread infection in humans and many other species of warm–blooded animals. Toxoplasma gondii-derived heat shock protein 70 (Hsp70) may play an important role in the virulence of Toxoplasma gondii (T. gondii). In the present study, T. gondii Hsp70 was amplified by polymerase chain reaction (PCR) from the DNA of the T. gondiitachyzoite RH strain through the use o...
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A 30 kDa protein was purified from pig liver cytosol by using ATP-Sepharose and Green A column chromatography. The partial amino acid sequences of the protein (95 amino acid residues) had no similarity with any proteins recorded in data banks. The protein was able to form a stable complex with unfolded dihydrofolate reductase (DHFR). The spontaneous refolding of chemically denatured DHFR was ar...
متن کاملATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation.
ATP-binding cassette (ABC) transporters couple ATP binding and hydrolysis to the movement of substances across the membrane; conformational changes clearly play an important role in the transporter mechanism. Previously, we have shown that a dimer of MalK, the ATPase subunit of the maltose transporter from Escherichia coli, undergoes a tweezers-like motion in a transport cycle. The MalK monomer...
متن کاملIn Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis
Heat shock protein 90 (Hsp90), an abundant molecular chaperone in the eukaryotic cytosol, is involved in the folding of a set of cell regulatory proteins and in the re-folding of stress-denatured polypeptides. The basic mechanism of action of Hsp90 is not yet understood. In particular, it has been debated whether Hsp90 function is ATP dependent. A recent crystal structure of the NH2-terminal do...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2004
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20031680