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Dual substrate‐controlled kinase activity leads to polyphosphorylated lasso peptides
Author(s) -
Zhu Shaozhou,
Fage Christopher D.,
Hegemann Julian D.,
Yan Dushan,
Marahiel Mohamed A.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12386
Subject(s) - peptide , biochemistry , kinase , lasso (programming language) , peptide sequence , chemistry , computational biology , biology , gene , computer science , world wide web
Lasso peptides are characterized by their peculiar lariat knot‐like structure. Except for maturation of this fold, post‐translational modifications of lasso peptides are rare. However, we recently delineated the biosynthetic pathway of a post‐translationally phosphorylated lasso peptide, paeninodin. In this study, further investigation of two kinases revealed their ability to transfer multiple phosphate groups onto precursor peptide substrates, ultimately leading to polyphosphorylated lasso peptides. We found that this polyphosphorylating activity depended on the identity of the phosphate donor and the sequence of the precursor peptide. Our investigations provide new insight into the remarkable strategies for chemical diversification employed by the lasso peptide biosynthetic machinery.