Identification of Chaperonin Particles in Mammalian Brain Cytosol and of T‐Complex Polypeptide 1 as One of Their Components
- 1 June 1993
- journal article
- Published by Wiley in Journal of Neurochemistry
- Vol. 60 (6) , 2327-2330
- https://doi.org/10.1111/j.1471-4159.1993.tb03524.x
Abstract
An approximately 950-kDa heteromeric particle was purified from guinea-pig and rat brain by sucrose gradient fractionation of post-mitochondrial supernatants. Further purification, by affinity chromatography on ATP-Sepharose and anion exchange FPLC on MonoQ, yielded a particle with typical chaperonin ultrastructure. One of the component polypeptides was recognized by a monoclonal antibody to murine T-complex polypeptide 1. Brain cytosolic chaperonin particles formed a binary complex with unfolded tubulin subunits. The polypeptide compositions of the cytosolic chaperonin particles appeared very similar between brain and testicular tissues of the same animal, but differed subtly between the guinea-pig and rat.Keywords
This publication has 10 references indexed in Scilit:
- TCP1 complex is a molecular chaperone in tubulin biogenesisNature, 1992
- T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosolNature, 1992
- A cytoplasmic chaperonin that catalyzes β-actin foldingPublished by Elsevier ,1992
- Protein folding in the cellNature, 1992
- Molecular Chaperones: The Plant ConnectionScience, 1990
- Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodiesJournal of Cell Science, 1989
- The t complex polypeptide 1 (TCP-1) is associated with the cytoplasmic aspect of Golgi membranesCell, 1989
- The structure of the largest murine neurofilament protein (NF-H) as revealed by cDNA and genomic sequencesMolecular Brain Research, 1988
- Two-stage expression of neurofilament polypeptides during rat neurogenesis with early establishment of adult phosphorylation patternsJournal of Neuroscience, 1987
- A protein factor essential for microtubule assembly.Proceedings of the National Academy of Sciences, 1975