A novel testis-specific 105-kDa protein related to the 90-kDa heat-shock protein
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چکیده
منابع مشابه
Reactive cysteines of the 90-kDa heat shock protein, Hsp90.
The 90-kDa heat shock protein (Hsp90) is the most abundant molecular chaperone of the eukaryotic cytoplasm. Its cysteine groups participate in the interactions of Hsp90 with the heme-regulated eIF-2alpha kinase and molybdate, a stabilizer of Hsp90-protein complexes. In our present studies we investigated the reactivity of the sulfhydryl groups of Hsp90. Our data indicate that Hsp90 as well as t...
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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...
متن کاملA novel 29-kDa chicken heat shock protein.
The family of small heat shock proteins is the more variable among the highly conserved superfamily of heat shock proteins (HSP). Using a metabolic labeling procedure with tissue explants, we have detected in chickens a new member of the small HSP family with an apparent molecular weight of 29-kDa. This protein was induced in broiler chickens' heart muscle and lungs following an in vivo heat st...
متن کاملThe 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 ...
متن کاملCalmodulin-regulated binding of the 90-kDa heat shock protein to actin filaments.
We have found that the 90-kDa heat shock protein (HSP90) prepared from a mouse lymphoma exists in homodimeric form under physiological conditions and has the ability to bind to F-actin (Koyasu, S., Nishida, E., Kadowaki, T., Matsuzaki, F., Iida, K., Harada, F., Kasuga, M., Sakai, H., and Yahara, I. (1986) Proc. Natl. Acad. Sci. U.S.A., in press). Here we show that calmodulin regulates the bindi...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1990
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1990.tb19356.x