Phage T4 homologous strand exchange: a DNA helicase, not the strand transferase, drives polar branch migration

Article Abstract:

Reconstruction of a multiprotein complex made of five bacteriophage T4 proteins shows that strand transferases are necessary for homologous DNA pairing in vivo and branch migration is mediated by DNA helicase. The UvsY protein is required for homologous pairing but it inhibits branch migration mediated by the UvsX protein. Polar branch migration is dependent DNA helicase and an accessory protein.

DNA repair, Transferases

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Keeping transcriptional activators under control

Article Abstract:

The available data suggests that rapid and slower mechanisms that modulate the stability of promoter-bound transcription complexes exist. Some of these mechanisms involve the proteasome, others do not but different activators employ these mechanisms to different extents leading a wide spectrum of dynamic behaviors of activator-promoter complexes within cells.

Science & research, Genetic transcription, Transcription (Genetics), Cellular control mechanisms, Cell regulation, Ubiquitin-proteasome system

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• Abstracts: The acidic activation domains of the GCN4 and GAL4 proteins are not alpha-helical but form beta sheets. Genetic evidence that an activation domain of GAL4 does not require acidity and may form a beta sheet

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