ArticleProtein science : a publication of the Protein Society2001
Proteins of circularly permuted sequence present within the same organism: the major serine proteinase inhibitor from Capsicum annuum seeds.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Article
- Integrative metabolomic and transcriptomic analysis provides insight into the mechanism of pigmentation in potato tuber eyes.BMC plant biology · 2025Article
- Unveiling mechanisms of antimicrobial peptide: Actions beyond the membranes disruption.Heliyon · 2024Review
- A Multifunctional Trypsin Protease Inhibitor from Yellow Bell Pepper Seeds: Uncovering Its Dual Antifungal and Hypoglycemic Properties.Pharmaceutics · 2023Article
- Transcriptome Analysis of Capsicum Chlorosis Virus-Induced Hypersensitive Resistance Response in Bell Capsicum.PloS one · 2016Article
- Characterization of Peptides from Capsicum annuum Hybrid Seeds with Inhibitory Activity Against α-Amylase, Serine Proteinases and Fungi.The protein journal · 2015Article
- Stress inducible proteinase inhibitor diversity in Capsicum annuum.BMC plant biology · 2012Article
- CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships.Genome biology · 2008Article
- Tandem duplication, circular permutation, molecular adaptation: how Solanaceae resist pests via inhibitors.BMC bioinformatics · 2008Article
- Manipulation of endogenous trypsin proteinase inhibitor production in Nicotiana attenuata demonstrates their function as antiherbivore defenses.Plant physiology · 2004Article
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7 authors.
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Abstract
The major serine proteinase inhibitor from bell pepper (Capsicum annuum, paprika) seeds was isolated, characterized, and sequenced, and its disulfide bond topology was determined. PSI-1.2 is a 52-amino-acid-long, cysteine-rich polypeptide that inhibits both trypsin (K(i) = 4.6 x 10(-9) M) and chymotrypsin (K(i) = 1.1 x 10(-8) M) and is a circularly permuted member of the potato type II inhibitor family. Mature proteins of this family are produced from precursor proteins containing two to eight repeat units that are proteolytically cleaved within, rather than between, the repeats. In contrast, PSI-1.2 corresponds to a complete repeat that was predicted as the putative ancestral protein of the potato type II family. To our knowledge, this is the first case in which two proteins related to each other by circular permutation are shown to exist in the same organism and are expressed within the same organ. PSI-1.2 is not derived from any of the known precursors, and it contains a unique amphiphilic segment in one of its loops. A systematic comparison of the related precursor repeat-sequences reveals common evolutionary patterns that are in agreement with the ancestral gene-duplication hypothesis.
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