ArticleJournal of molecular evolution1994
Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop.
Article in Journal of molecular evolution, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Subtilisin inhibitor like protein '3 Biotech · 2018Article
- Expression of various biotin-binding proteins in transgenic tobacco confers resistance to potato tuber moth, Phthorimaea operculella (Zeller) (fam. Gelechiidae).Transgenic research · 2010Article
- Serine protease inhibitors specifically defend Solanum nigrum against generalist herbivores but do not influence plant growth and development.The Plant cell · 2010Article
- Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem.Protein science : a publication of the Protein Society · 2003Article
- Avidin expressed in transgenic tobacco leaves confers resistance to two noctuid pests, Helicoverpa armigera and Spodoptera litura.Transgenic research · 2002Article
- Expression of biotin-binding proteins, avidin and streptavidin, in plant tissues using plant vacuolar targeting sequences.Transgenic research · 2002Article
- Cloning and characterization of a trypsin inhibitor cDNA from amaranth (Amaranthus hypochondriacus) seeds.Plant molecular biology · 1999Article
- Prosystemin from potato, black nightshade, and bell pepper: primary structure and biological activity of predicted systemin polypeptides.Plant molecular biology · 1998Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A protein phylogenetic tree was constructed from 24 homologous proteinase inhibitor I sequences identified in the EMBL/Genbank and Swiss-Prot databases and from translated amino acid data from four constitutive cDNA clones of proteinase inhibitor I characterized from potato tuber mRNA. The tree suggests that divergence of at least four paralogous proteins with functional specialization occurred at different times during the evolutionary history of the proteinase inhibitor I family. Five distinct regions in the primary structure, earlier identified by structural studies, were used to analyze the inhibitor family for hypervariability (Creighton and Darby, Trends Biochem Sci 14:319-324, 1989). Mutations did not occur with higher-than-random frequency within the proteinase binding region. When isoinhibitor, orthologous, or paralogous data subsets were subsequently analyzed the same results were obtained. Comparison of the amino acid sequences for all the known potato proteinase isoinhibitor I proteins identified ten highly variable sites. These also were distributed randomly. Thus hypervariability, which has been observed in all other serine proteinase inhibitor families to date, appears to be lacking in the proteinase inhibitor I family.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.