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Discovery and characterization of Rubrinodin provide clues into the evolution of Lasso peptides
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Xiu, Huanhuan, Wang, Mengjiao, Fage, Christopher, He, Yile, Niu, Xiaogang, Han, Meng, Li, Fei, An, Xiaoping, Fan, Huahao, Song, Lihua, Zheng, Guojun, Zhu, Shaozhou and Tong, Yigang (2022) Discovery and characterization of Rubrinodin provide clues into the evolution of Lasso peptides. Biochemistry, 61 (7). pp. 595-607. doi:10.1021/acs.biochem.2c00029 ISSN 1520-4995.
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Official URL: https://doi.org/10.1021/acs.biochem.2c00029
Abstract
Lasso peptides are unique natural products that comprise a class of ribosomally synthesized and post-translationally modified peptides. Their defining three-dimensional structure is a lariat knot, in which the C-terminal tail is threaded through a macrolactam ring formed between the N-terminal amino group and an Asp or Glu side chain (i.e., an isopeptide bond). Recent genome mining strategies have revealed various types of lasso peptide biosynthetic gene clusters and have thus redefined the known chemical space of lasso peptides. To date, over 20 different types of these gene clusters have been discovered, including several different clades from Proteobacteria. Despite the diverse architectures of these gene clusters, which may or may not encode various tailoring enzymes, most currently known lasso peptides are synthesized by two discrete clades defined by the presence of an ATP-binding cassette transporter or its absence and (sometimes) concurrent appearance of an isopeptidase, raising questions about their evolutionary history. Herein, we discovered and characterized the lasso peptide rubrinodin, which is assembled by a gene cluster encoding both an ATP-binding cassette transporter and an isopeptidase. Our bioinformatics analyses of this and other representative cluster types provided new clues into the evolutionary history of lasso peptides. Furthermore, our structural and biochemical investigations of rubrinodin permitted the conversion of this thermolabile lasso peptide into a more thermostable scaffold.
Item Type: | Journal Article | ||||||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||||||
SWORD Depositor: | Library Publications Router | ||||||||
Journal or Publication Title: | Biochemistry | ||||||||
Publisher: | American Chemical Society (ACS) | ||||||||
ISSN: | 1520-4995 | ||||||||
Official Date: | 5 April 2022 | ||||||||
Dates: |
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Volume: | 61 | ||||||||
Number: | 7 | ||||||||
Page Range: | pp. 595-607 | ||||||||
DOI: | 10.1021/acs.biochem.2c00029 | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Reuse Statement (publisher, data, author rights): | ** From Crossref journal articles via Jisc Publications Router ** History: epub 17-03-2022; issued 17-03-2022. | ||||||||
Access rights to Published version: | Restricted or Subscription Access |
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