Giant proteins with flour power

Article Abstract:

Field-flow fractionation studies of glutenin proteins reveal their enormous size comparable to a muscle protein, titin, and their unique viscoelastic properties. The glutenin polypeptide comprises of repeating sequences of glutamine, proline and glycine. The proteins achieve their giant sizes through formation of disulphide-linked polymers of discrete polypeptides. This imparts springiness to the wheat dough whereas a complex mixture of gliadin monomers provides the plasticizer property. These properties make wheat flour eminently suitable for bread-making.

Analysis, Reports, Proteins, Flour, Protein structure, Plant proteins

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Reversal of fortune for nascent proteins

Article Abstract:

The mechanism evolved by DNA viruses such as adenovirus and cytomegalovirus to prevent their detection by the hosts' immune systems is similar to the cellular mechanism of eliminating abnormal synthesized proteins. Proteins that fail to fold properly are retained in the endoplasmic reticulum. Reverse translocation transports these proteins back into the cytosol, where they are degraded. The proteins are deglycosylated, released from the endoplasmic membrane and polyubiquitinated. The 26S proteasome performs the final protein degradation.

Observations, Endoplasmic reticulum, Proteolysis, DNA viruses

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Glucosylation of Rho proteins by Clostridium difficile toxin B

Article Abstract:

The cytotoxin Clostridium difficile toxin B is a monoglucosyltransferase that catalyzes the injection of glucose in threonine 37 of RhoA. When the glycosylated RhoA are induced in monolayer cells, the actin filaments are separated which reflects a dominant-negative activity of glycosylated RhoA. The monoglucosylation reaction is a causative factor in antibiotic-associated pseudomembranous colitis.

Serum, Blood serum, Glycosylation

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