An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation

Article Abstract:

A domain of the tetanus toxin antigen TTCF with disrupted lysosomes isolated from the Epstein-Barr virus (EV) was incubated to examine processing of a foreign antigen. The major TTCF digestion products were sequenced and five major asparagine residues arose from three cleavages. This suggested that B-cell lysosomes have unusual cysteine endopeptidases which have potential specificity for asparagine. It is possible that non-glycosylated microbial proteins including TTCF are more sensitive to processing by AEP.

Antigens

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A new protease required for cell-cycle progression in yeast

Article Abstract:

Ulp1, a yeast ubiquitin-like (Ubl)-specific protease, has been found to cleave proteins from the yeast protein Smt3 and the vertebrate Ubl protein SUMO-1. However, it does not cleave proteins from ubiquitin. It was established that Ulp1-mediated Smt3-protein deconjugation is needed for cell-cycle progression. This has similarities with the need for timed phosphorylation and dephosphorylation of cell-cycle proteins.

Yeast, Yeast (Food product)

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Unfolded conformations of alpha-lytic protease are more stable than its native state

Article Abstract:

The extracellular bacterial protease alpha-lytic (alphaLP) is synthesized with a large amino-terminal pro-region that is necessary for its folding. The protease folds to an inactive, partially folded state, I, in the absence of the pro-region. The native state N is separated from I, and it is shown that I and fully unfolded states of alphaLP have less free energy than the native state.

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