Albumins and their processing machinery are hijacked for cyclic peptides in sunflower

被引：121

作者：

Mylne, Joshua S. ^{[1
]}

Colgrave, Michelle L. ^{[2
]}

Daly, Norelle L. ^{[1
]}

Chanson, Aurelie H. ^{[1
]}

Elliott, Alysha G. ^{[1
]}

McCallum, Emily J. ^{[1
]}

Jones, Alun ^{[1
]}

Craik, David J. ^{[1
]}

机构：

[1] Univ Queensland, Inst Mol Biosci, Brisbane, Qld, Australia

[2] Commonwealth Sci & Ind Res Org Livestock Ind, Brisbane, Qld, Australia

来源：

NATURE CHEMICAL BIOLOGY | 2011年 / 7卷 / 05期

基金：

美国国家科学基金会; 美国农业部;

关键词：

SEED STORAGE PROTEINS; TRYPSIN-INHIBITOR; ARABIDOPSIS-THALIANA; PROTEASE INHIBITORS; SERINE-PROTEASE; ENZYME; POTENT; ENDOPEPTIDASE; BIOSYNTHESIS; PROPEPTIDES;

D O I：

10.1038/nchembio.542

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cyclic peptide sunflower trypsin inhibitor 1 (SFTI-1) blocks trypsin and is a promising drug lead and protein engineering scaffold. We show that SFTI-1 and the newfound SFT-L1 are buried within PawS1 and PawS2, precursors for seed storage protein albumins. Proalbumins are matured by asparaginyl endopeptidase, which we show is required to liberate both ends of SFTI-1 as well as to mature PawS1 albumin. Thus, these peptides emerge from within an albumin precursor by the action of albumin's own processing enzyme.

引用

页码：257 / 259

页数：3

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