A [3Fe-4S] cluster and tRNA-dependent aminoacyltransferase BlsK in the biosynthesis of Blasticidin S
| Autor: | Yuchun Zhao, Aiqin Du, Xiankun Wang, Xiangkun Luo, Yaojie Gao, T. Mark Zabriskie, Zixin Deng, Xinyi He, Ming Jiang |
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| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Iron-Sulfur Proteins Arginine Hypothetical protein RNA Transfer Amino Acyl 010402 general chemistry 01 natural sciences Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Biosynthesis Bacterial Proteins Multidisciplinary Chemistry Aminoacyltransferase RNA hemic and immune systems Nucleosides Methylation Biological Sciences Aminoacyltransferases Streptomyces 0104 chemical sciences Blasticidin S Biosynthetic Pathways 030104 developmental biology Biochemistry Transfer RNA |
| Zdroj: | Proc Natl Acad Sci U S A |
| ISSN: | 1091-6490 |
| Popis: | Blasticidin S is a peptidyl nucleoside antibiotic. Its biosynthesis involves a cryptic leucylation and two leucylated intermediates, LDBS and LBS, have been found in previous studies. Leucylation has been proposed to be a new self-resistance mechanism during blasticidin S biosynthesis, and the leucyl group was found to be important for the methylation of β-amino group of the arginine side chain. However, the responsible enzyme and its associated mechanism of the leucyl transfer process remain to be elucidated. Here, we report results investigating the leucyl transfer step forming the intermediate LDBS in blasticidin biosynthesis. A hypothetical protein, BlsK, has been characterized by genetic and in vitro biochemical experiments. This enzyme catalyzes the leucyl transfer from leucyl-transfer RNA (leucyl-tRNA) to the β-amino group on the arginine side chain of DBS. Furthermore, BlsK was found to contain an iron-sulfur cluster that is necessary for activity. These findings provide an example of an iron-sulfur protein that catalyzes an aminoacyl-tRNA (aa-tRNA)-dependent amide bond formation in a natural product biosynthetic pathway. |
| Databáze: | OpenAIRE |
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