Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin
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چکیده
منابع مشابه
The production of molecular clones of Toxoplasma gondii-derived heat shock protein 70 kDa
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 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein
The 25-kD inhibitor of actin polymerization (25-kD IAP), isolated from turkey smooth muscle (Miron, T., M. Wilchek, and B. Geiger, 1988. Eur. J. Biochem. 178:543-553), is shown here to be a low molecular mass heat shock protein (HSP). Direct sequence analysis of the purified protein, as well as cloning and sequencing of the respective cDNA, disclosed a high degree of homology (67% identity, 80%...
متن کاملDefined sequence segments of the small heat shock proteins HSP25 and alphaB-crystallin inhibit actin polymerization.
The interaction of small heat shock proteins (sHSPs) with the actin cytoskeleton has been described and some members of this family, e.g. chicken and murine HSP25 (HSP27), inhibit the polymerization of actin in vitro. To analyse the molecular basis of this interaction, we synthesized a set of overlapping peptides covering the complete sequence of murine HSP25 and tested the effect of these pept...
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The 90 kDa heat shock protein (Hsp90) is a major cytoplasmic molecular chaperone associating with numerous other proteins. Both genetic and in vitro refolding experiments using reticulocyte lysate have suggested a functional interaction of Hsp90 with yeast human homologues of E. coli DnaJ. Here we present direct evidence using surface plasmon resonance that Hsp90 and the human DnaJ homologue, H...
متن کاملMolecular characterization of Oryza sativa 16.9 kDa heat shock protein.
A rice class I low-molecular-mass heat shock protein (LMM HSP) Oshsp 16.9 was overexpressed in Escherichia coli. Oligomerized complexes of Oshsp16.9 were harvested and electron microscopic observations of purified complexes revealed globular structures of 10-20 nm in diameter (with majority of 15-18 nm) and calculated to comprise approx. 12 monomers per complex. In comparison, complexes from na...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2003
ISSN: 0014-2956
DOI: 10.1046/j.1432-1033.2003.03449.x