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Updated: May 9, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
Expanding the structural diversity of polyketides by exploring the cofactor tolerance of an inline methyltransferase
Jaclyn M Winter1, Grace Chiou, Ian R Bothwell
1Department of Chemical and Biomolecular Engineering, University of California, Los Angeles, California 90095, USA.
Abstract:
A strategy for introducing structural diversity into polyketides by exploiting the promiscuity of an in-line methyltransferase domain in a multidomain polyketide synthase is reported. In vitro investigations using the highly-reducing fungal polyketide synthase CazF revealed that its methyltransferase domain accepts the nonnatural cofactor propargylic Se-adenosyl-l-methionine and can transfer the propargyl moiety onto its growing polyketide chain. This propargylated polyketide product can then be further chain-extended and cyclized to form propargyl-α pyrone or be processed fully into the alkyne-containing 4'-propargyl-chaetoviridin A.
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