Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways

Article Abstract:

Molecular biological techniques were used to study the receptor binding activity of Pex14p, an S. cerevisiae peroxin that is attached to the outer face of the peroxisomal membrane which has been known as a component of the protein import machinery. The results showed that Pex14p binds to the N-terminal peroxisomal targeting signal (PTS2) receptor Pex7p, the C-terminal PTS1 receptor Pex5p, and to the putative docking protein for PTS1-dependent protein import, Pex13p. Such findings indicate that Pex14p is a component of both PTS1- and PTS2-dependent protein import pathways in the peroxisomal membrane.

Usage, Membrane proteins, Fluorescence microscopy, Cloning, Electron microscopy, Immunoassay, Enzymatic analysis

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ATP binding to the sigma54-dependent activator XylR triggers a protein multimerization cycle catalyzed by UAS DNA

Article Abstract:

Previous research has shown that ATP hydrolysis plays a major role in the activation of sigma54-dependent promoters. In the case of the activator XylR, ATP binding, aside from activating the polymerase to initiate transcription, triggers a protein multimerization cycle catalyzed by upstream activating sequence DNA. This cycle is possibly present in all sigma54-dependent regulators as well.

Promoters (Genetics), Adenosine triphosphate, ATP

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