Identification and characterization of a novel spermidine/spermine acetyltransferase encoded by gene ste26 from Streptomyces sp. 139

Biochimie ◽  
2011 ◽  
Vol 93 (9) ◽  
pp. 1401-1407 ◽  
Author(s):  
Liping Bai ◽  
Ming Chang ◽  
Junjie Shan ◽  
Rong Jiang ◽  
Yang Zhang ◽  
...  
Molecules ◽  
2021 ◽  
Vol 26 (21) ◽  
pp. 6580
Author(s):  
Charlotte Beck ◽  
Tetiana Gren ◽  
Francisco Javier Ortiz-López ◽  
Tue Sparholt Jørgensen ◽  
Daniel Carretero-Molina ◽  
...  

Streptomyces are well-known producers of a range of different secondary metabolites, including antibiotics and other bioactive compounds. Recently, it has been demonstrated that “silent” biosynthetic gene clusters (BGCs) can be activated by heterologously expressing transcriptional regulators from other BGCs. Here, we have activated a silent BGC in Streptomyces sp. CA-256286 by overexpression of a set of SARP family transcriptional regulators. The structure of the produced compound was elucidated by NMR and found to be an N-acetyl cysteine adduct of the pyranonaphtoquinone polyketide 3′-O-α-d-forosaminyl-(+)-griseusin A. Employing a combination of multi-omics and metabolic engineering techniques, we identified the responsible BGC. These methods include genome mining, proteomics and transcriptomics analyses, in combination with CRISPR induced gene inactivations and expression of the BGC in a heterologous host strain. This work demonstrates an easy-to-implement workflow of how silent BGCs can be activated, followed by the identification and characterization of the produced compound, the responsible BGC, and hints of its biosynthetic pathway.


2020 ◽  
Author(s):  
Ling Liu ◽  
Sainan Li ◽  
Runze Sun ◽  
Xiangjing Qin ◽  
Jianhua Ju ◽  
...  

<p> Bohemamines (BHMs) are bacterial alkaloids containing a pyrrolizidine core with two unprecedented methyl groups. Herein we report the activation of BHMs biosynthesis in <i>Streptomyces </i>sp. CB02009 using a ribosome engineering approach. Identification and characterization of the <i>bhm</i> gene cluster reveals a coordinated action of nonribosomal peptide synthetase BhmJ, Baeyer-villiger monooxygenase BhmK and methyltransferase BhmG for BHMs biosynthesis. BhmG is responsible for the C-methylation on C-7, while the C-9 methyl group is from a non-proteinogenic amino acid (2<i>S</i>,5<i>S</i>)-5-methylproline, required for BHMs production in three model <i>Streptomyces </i>hosts. Our study shed light on the intricate interaction of BhmJ/BhmK/BhmG for the economical biosynthesis of BHMs in their native producer, and also unraveled that BhmJ and BhmK are competent biocatalysts in <i>S</i><i>treptomyce </i><i>albus</i>.</p>


2012 ◽  
Vol 30 (1) ◽  
pp. 202-209 ◽  
Author(s):  
Ji-Hye Nah ◽  
Shin-Hae Park ◽  
Hye-Mi Yoon ◽  
Si-Sun Choi ◽  
Chul-Hoon Lee ◽  
...  

2011 ◽  
Vol 35 (8) ◽  
pp. 477-486 ◽  
Author(s):  
Saeed Sadigh-Eteghad ◽  
Alireza Dehnad ◽  
Dariush Shanebandi ◽  
Iraj Khalili ◽  
Nasser Razmarayii ◽  
...  

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