Localization of mitochondrial Hsp56 chaperonin during sea urchin development.

Abstract

We have previously demonstrated that Paracentrotus lividus nuclear genome encodes for the heat shock inducible chaperonin homolog Hsp 56 (1) and that the mature protein is localized in the mitochondrial matrix (2). In this paper we report that constitutive Hsp56 is maternally inherited, in fact it is present in the in unfertilized eggs, and that it has a perinuclear specific localization during cleavage. In the later stages both the constitutive and the heat shock inducible chaperonin has a specific territorial distribution. Moreover following heat shock, the Hsp56 appears in the cytoplasm and in the postmitochondrial supernatant beside the mitochondrial fraction.

• Authors: M C Roccheri, M Patti, M Agnello, F Gianguzza, E Carra, A M Rinaldi
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 287 Issue 5 Pg. 1093-8 (Oct 12 2001) ISSN: 0006-291X [Print] United States
• PMID: 11587534 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright 2001 Academic Press.

Chemical References

• Molecular Chaperones
• Tacrolimus Binding Proteins
• tacrolimus binding protein 4

Topics

• Animals
• Blotting, Western
• Cell Fractionation
• Embryo, Nonmammalian (chemistry, ultrastructure)
• Immunohistochemistry
• Mitochondria (chemistry)
• Molecular Chaperones (isolation & purification)
• Sea Urchins
• Tacrolimus Binding Proteins (isolation & purification)