Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy

Article Abstract:

Researchers have used quick-freeze/deep-etch electron microscopy of recombinant proteins adsorbed to mica to investigate the oligomeric ATPase NSF. It was found that NSF, whose hydrolytic activity is vital for membrane fusion, is a hollow 10 nm x 16 nm cylinder. Its conformation is determined by nucleotide binding. It was possible to show that conformational changes take place in NSF during its ATPase cycle. Researchers also assessed the structure and geometry of the SNAP receptors which are dissociated by NSF.

Membrane fusion

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Membrane traffic: what drives the AAA motor?

Article Abstract:

ATPases associated with a variety of cellular activities (AAA)-ATPases are involved in ATP binding, hydrolysis, and release and these are mediated by conformational changes propagated from enzyme to substrate. Data indicate that a p97-catalyzed conformational transformation in these AAA-ATpases is driven by a molecular "ratchet" consisting of D1 and D2 domains.

Enzymes, Conformational analysis, Enzyme structure-activity relationships

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Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin

Article Abstract:

Research shows that the histone variant H2A.Z is enriched in euchromatic regions of the chromatin, which in association with a boundary elelment prevents spread of heterochromatin, indicating euchromatin and heterochromain possess components that block switching to the opposite chromatin state.

Physiological aspects, Genetic aspects, Histones, Eukaryotes, Chromatin, Structure

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