ArticleProceedings of the National Academy of Sciences of the United States of America1999
Ovochymase, a Xenopus laevis egg extracellular protease, is translated as part of an unusual polyprotease.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 36 citations in OpenAlex.
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- Identification of differentially expressed genes in American cockroach ovaries and testes by suppression subtractive hybridization and the prediction of its miRNAs.Molecular genetics and genomics : MGG · 2013Article
- Cell surface changes in the egg at fertilization.Molecular reproduction and development · 2009Review
- Bimodal protein targeting through activation of cryptic mitochondrial targeting signals by an inducible cytosolic endoprotease.Molecular cell · 2008Article
- Identification and characterization of human polyserase-3, a novel protein with tandem serine-protease domains in the same polypeptide chain.BMC biochemistry · 2006Article
- Cloning and analysis of a cDNA encoding a putative serine protease comprising two trypsin-like domains of Trichinella spiralis.Parasitology research · 2006Article
- Polyserase-I, a human polyprotease with the ability to generate independent serine protease domains from a single translation product.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Ovochymase, an extracellular Xenopus laevis egg serine active-site protease with chymotrypsin-like (Phe-X) substrate specificity, is released during egg activation. Molecular cloning results revealed that ovochymase is translated as part of an unusual polyprotein proenzyme. In addition to the ovochymase protease domain at the C terminus of the deduced amino acid sequence, two unrelated serine protease domains were present, each with apparent trypsin-like (Arg/Lys-X) substrate specificity, and thus, they were designated ovotryptase1 (at the N terminus) and ovotryptase2 (a mid domain). Also, a total of five CUB domains were interspersed between the protease domains. The presence of a hydrophobic signal sequence indicated that the polyprotein was secreted. Immunolocalization and Western blot studies of all three proteases showed that they are all present in the perivitelline space of unactivated eggs, apparently as proenzymes processed away from the original polyprotein. Western blot analysis also showed that the vast majority of the proteases in ovary, eggs, and embryos were present as the proenzyme forms, suggesting that the functions of these proteases depend on very limited levels of activation.
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