Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form

Article Abstract:

The transformation of toxins from a water-soluble protein to a membrane pore was analyzed to charcaterize the mechanisms of protein insertion and channel formation. Crystallographic analysis of perfringolysin O (PFO) thiol-activated cytolysin via multiple isomorphous replacement indicated the presence of 11 alpha helices and two helices with varying numbers of amino acid residues. The membrane insertion of thiol-activated cytolysins was dependent on the receptor which revealed the hydrophobic loop and masked the polar regions for membrane insertion.

Analysis, Cell membranes, Toxins

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Multiple TATA-binding factors come back into style

Article Abstract:

Eukaryotic transcription has long been discovered and recent advancements were made basing from TATA sequence and other basal promoters which were believed to be capable of binding with multiple factors. Among these factors are the multiple TFIID factors which bind with a TATA-binding protein (TBP) and result to a TBP-containing complex. Multiple TFIID factors together with 50 proteins from RNA polymerase II transcription apparatus contribute to the genetic activities involved in the metazoan life.

Eukaryotic cells, Cells (Biology), Eukaryotes

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