A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein

Marcus C.S. Lee; Martin J. Scanlon; David J. Craik; Marilyn A. Anderson

doi:10.1038/9293

A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein

Marcus C.S. Lee, Martin J. Scanlon, David J. Craik, Marilyn A. Anderson (Lead / Corresponding author)

Biological Chemistry and Drug Discovery

Research output: Contribution to journal › Article › peer-review

58 Citations (Scopus)

Abstract

Female reproductive tissues of the ornamental tobacco amass high levels of serine proteinase inhibitors (PIs) for protection against pests and pathogens. These PIs are produced from a precursor protein composed of six repeats each with a protease reactive site. Here we show that proteolytic processing of the precursor generates five single-chain PIs and a remarkable two-chain inhibitor formed by disulfide-bond linkage of N- and C-terminal peptide fragments. Surprisingly, PI precursors adopt this circular structure regardless of the number of inhibitor domains, suggesting this bracelet-like conformation is characteristic of the widespread potato inhibitor II (Pot II) protein family.

Original language	English
Pages (from-to)	526-530
Number of pages	5
Journal	Nature Structural Biology
Volume	6
Issue number	6
DOIs	https://doi.org/10.1038/9293
Publication status	Published - Jun 1999

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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title = "A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein",

abstract = "Female reproductive tissues of the ornamental tobacco amass high levels of serine proteinase inhibitors (PIs) for protection against pests and pathogens. These PIs are produced from a precursor protein composed of six repeats each with a protease reactive site. Here we show that proteolytic processing of the precursor generates five single-chain PIs and a remarkable two-chain inhibitor formed by disulfide-bond linkage of N- and C-terminal peptide fragments. Surprisingly, PI precursors adopt this circular structure regardless of the number of inhibitor domains, suggesting this bracelet-like conformation is characteristic of the widespread potato inhibitor II (Pot II) protein family.",

author = "Lee, {Marcus C.S.} and Scanlon, {Martin J.} and Craik, {David J.} and Anderson, {Marilyn A.}",

note = "Funding Information: We thank G.M. Neumann and R. Condron for electrospray mass spectrometry and N-terminal sequencing analysis, and E.A. Miller, T.J. Lithgow, N.J. Hoogenraad and A.E. Clarke for critical reading of the manuscript. This work was supported by a grant from the Australian Research Council. D.J.C. is an Australian Research Council Senior Fellow.",

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T1 - A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein

AU - Lee, Marcus C.S.

AU - Scanlon, Martin J.

AU - Craik, David J.

AU - Anderson, Marilyn A.

N1 - Funding Information: We thank G.M. Neumann and R. Condron for electrospray mass spectrometry and N-terminal sequencing analysis, and E.A. Miller, T.J. Lithgow, N.J. Hoogenraad and A.E. Clarke for critical reading of the manuscript. This work was supported by a grant from the Australian Research Council. D.J.C. is an Australian Research Council Senior Fellow.

PY - 1999/6

Y1 - 1999/6

N2 - Female reproductive tissues of the ornamental tobacco amass high levels of serine proteinase inhibitors (PIs) for protection against pests and pathogens. These PIs are produced from a precursor protein composed of six repeats each with a protease reactive site. Here we show that proteolytic processing of the precursor generates five single-chain PIs and a remarkable two-chain inhibitor formed by disulfide-bond linkage of N- and C-terminal peptide fragments. Surprisingly, PI precursors adopt this circular structure regardless of the number of inhibitor domains, suggesting this bracelet-like conformation is characteristic of the widespread potato inhibitor II (Pot II) protein family.

AB - Female reproductive tissues of the ornamental tobacco amass high levels of serine proteinase inhibitors (PIs) for protection against pests and pathogens. These PIs are produced from a precursor protein composed of six repeats each with a protease reactive site. Here we show that proteolytic processing of the precursor generates five single-chain PIs and a remarkable two-chain inhibitor formed by disulfide-bond linkage of N- and C-terminal peptide fragments. Surprisingly, PI precursors adopt this circular structure regardless of the number of inhibitor domains, suggesting this bracelet-like conformation is characteristic of the widespread potato inhibitor II (Pot II) protein family.

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A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein

Abstract

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