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Article
Molecular chaperones and the art of recognizing a lost cause
Molecular chaperones have long been heralded as machines for folding and salvaging proteins. However, not every attempt to fold or refold a protein can be successful. Chaperones are known to participate in the...
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Protocol
Purification of the Cytosolic ChaperoninTRiC from Bovine Testis
The chaperonins are oligomeric ring-complexes composed of ∼60 kDa sub- units, which mediate the folding of polypeptide chains in an ATP-dependent reaction (1). Class I chaperonins are found in prokaryotes and org...
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Protocol
Monitoring Actin Folding
Actin has been widely used as a model protein to study chaperone-mediated folding in vitro (1 2) and in vivo (3). In addition to being an essential and very abundant cytosolic protein, actin has the advantage of ...
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Protocol
Folding Assays
To determine the efficiency and rate of chaperone-mediated folding and renaturation, it is fundamental to have a good assay for the native conformation of the substrate protein. In the case of enzymes, the ide...
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Article
Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
The 62 kDa protein firefly luciferase folds very rapidly upon translation on eukaryotic ribosomes. In contrast, the chaperone-mediated refolding of chemically denatured luciferase occurs with significantly slo...
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Article
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein. The growing polypeptide interacts with a specific set of molecula...
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Article
Modulation of insulin induced ornithine decarboxylase by putrescine and methylputrescines in H-35 hepatoma cells
The effect of several methylputrescines on the activity of insulin-induced ornithine decarboxylase (ODC) was examined in H-35 hepatoma cells. The induction involved both protein and m-RNA synthesis. Actinomyci...
