期刊
NATURE CHEMISTRY
卷 9, 期 7, 页码 698-707出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.2714
关键词
-
资金
- European Research Council [617053]
- European Research Council (ERC) [617053] Funding Source: European Research Council (ERC)
Ribosomally synthesized peptides are built out of L-amino acids, whereas D-amino acids are generally the hallmark of nonribosomal synthetic processes. Here we show that the model bacterium Bacillus subtilis is able to produce a novel type of ribosomally synthesized and post-translationally modified peptide that contains D-amino acids, and which we propose to call epipeptides. We demonstrate that a two [4Fe-4S]-cluster radical S-adenosyl-L-methionine (SAM) enzyme converts L-amino acids into their D-counterparts by catalysing C-alpha-hydrogen-atom abstraction and using a critical cysteine residue as the hydrogen-atom donor. Unexpectedly, these D-amino acid residues proved to be essential for the activity of a peptide that induces the expression of LiaRS, a major component of the bacterial cell envelope stress-response system. Present in B. subtilis and in several members of the human microbiome, these epipeptides and radical SAM epimerases broaden the landscape of peptidyl structures accessible to living organisms.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据