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A 3‐hydroxy‐3‐methylglutaryl‐CoA synthase‐based probe for the discovery of the acyltransferase‐less type I polyketide synthases
Author(s) -
Liang Haoyu,
Jiang Lin,
Jiang Qiyun,
Shi Jie,
Xiang Jingxi,
Yan Xiaohui,
Zhu Xiangcheng,
Zhao Lixing,
Shen Ben,
Duan Yanwen,
Huang Yong
Publication year - 2019
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.14787
Subject(s) - biology , acyltransferase , polyketide , atp synthase , polyketide synthase , acyltransferases , computational biology , biochemistry , enzyme , biosynthesis
Summary Acyltransferase (AT)‐less type I polyketide synthases (PKSs) produce complex natural products due to the presence of many unique tailoring enzymes. The 3‐hydroxy‐3‐methylglutaryl coenzyme A synthases (HCSs) are responsible for β ‐alkylation of the growing polyketide intermediates in AT‐less type I PKSs. In this study, we discovered a large group of HCSs, closely associated with the characterized and orphan AT‐less type I PKSs through in silico genome mining, sequence and genome neighbourhood network analyses. Using HCS‐based probes, the survey of 1207 in‐house strains and 18 soil samples from different geographic locations revealed the vast diversity of HCS‐containing AT‐less type I PKSs. The presence of HCSs in many AT‐less type I PKSs suggests their co‐evolutionary relationship. This study provides a new probe to study the abundance and diversity of AT‐less type I PKSs in the environment and microbial strain collections. Our study should inspire future efforts to discover new polyketide natural products from AT‐less type I PKSs.