Protein folding in the central cavity of the GroEL-GroES chaperonin complex

Article Abstract:

A study was conducted on protein folding in the central cavity of the complex formed by the chaperonin GroEL and GroES, a single heptameric ring which binds asymmetrically to GroEL. GroEL was found to be capable of mediating folding minus a mechanistic requirement for the discharge of actively unfolded protein into free solution. Dissociations observed in non-native intermediates indicated leakage that may occur from the Gro-EL toroid in trans to GroES.

Protein folding

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Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex

Article Abstract:

A distinct group of ligand-dependent proteins, known as DRIPS, that interact with the vitamin D receptor, constitute a new cofactor complex. They bind to nuclear receptors and mediate ligand-dependent enhancement of transcription by VDR. The 13 DRIPS that make up the complex have been identified and it is shown that the complex is central to hormone-dependent transactivation by VDR on chromatin templates.

Genetic transcription, Transcription (Genetics)

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