Heterologous expression of Streptomyces clavuligerus ATCC 27064 cephamycin C gene cluster

2014 ◽  
Vol 186 ◽  
pp. 21-29 ◽  
Author(s):  
Y. Martínez-Burgo ◽  
R. Álvarez-Álvarez ◽  
R. Pérez-Redondo ◽  
P. Liras
2007 ◽  
Vol 189 (16) ◽  
pp. 5867-5874 ◽  
Author(s):  
Dylan C. Alexander ◽  
Cecilia L. Anders ◽  
Linda Lee ◽  
Susan E. Jensen

ABSTRACT Biosynthesis of cephamycin C in Streptomyces clavuligerus involves the initial conversion of lysine to α-aminoadipic acid. Lysine-6-aminotransferase and piperideine-6-carboxylate dehydrogenase carry out this two-step reaction, and genes encoding each of these enzymes are found within the cephamycin C gene cluster. However, while mutation of the lat gene causes complete loss of cephamycin production, pcd mutants still produce cephamycin at 30% to 70% of wild-type levels. Cephamycin production by pcd mutants could be restored to wild-type levels either by supplementation of the growth medium with α-aminoadipic acid or by complementation of the mutation with an intact copy of the pcd gene. Neither heterologous PCR nor Southern analyses showed any evidence for the presence of a second pcd gene. Furthermore, cell extracts from pcd mutants lack detectable PCD activity. Cephamycin production in the absence of detectable PCD activity suggests that S. clavuligerus must have some alternate means of producing the aminoadipyl-cysteinyl-valine needed for cephamycin biosynthesis.


2011 ◽  
Vol 46 (3) ◽  
pp. 811-816 ◽  
Author(s):  
Sheng Huang ◽  
Yudong Zhao ◽  
Zhiwei Qin ◽  
Xiaoling Wang ◽  
Mayca Onega ◽  
...  

ChemBioChem ◽  
2012 ◽  
Vol 13 (13) ◽  
pp. 1946-1952 ◽  
Author(s):  
Xiaoying Bian ◽  
Fan Huang ◽  
Francis A. Stewart ◽  
Liqiu Xia ◽  
Youming Zhang ◽  
...  

2021 ◽  
Author(s):  
Yang Liu ◽  
Haibo Zhou ◽  
Qiyao Shen ◽  
Guangzhi Dai ◽  
Fu Yan ◽  
...  

2021 ◽  
Vol 85 (3) ◽  
pp. 714-721
Author(s):  
Risa Takao ◽  
Katsuyuki Sakai ◽  
Hiroyuki Koshino ◽  
Hiroyuki Osada ◽  
Shunji Takahashi

ABSTRACT Recent advances in genome sequencing have revealed a variety of secondary metabolite biosynthetic gene clusters in actinomycetes. Understanding the biosynthetic mechanism controlling secondary metabolite production is important for utilizing these gene clusters. In this study, we focused on the kinanthraquinone biosynthetic gene cluster, which has not been identified yet in Streptomyces sp. SN-593. Based on chemical structure, 5 type II polyketide synthase gene clusters were listed from the genome sequence of Streptomyces sp. SN-593. Among them, a candidate gene cluster was selected by comparing the gene organization with grincamycin, which is synthesized through an intermediate similar to kinanthraquinone. We initially utilized a BAC library for subcloning the kiq gene cluster, performed heterologous expression in Streptomyces lividans TK23, and identified the production of kinanthraquinone and kinanthraquinone B. We also found that heterologous expression of kiqA, which belongs to the DNA-binding response regulator OmpR family, dramatically enhanced the production of kinanthraquinones.


2013 ◽  
Vol 56 (7) ◽  
pp. 619-627 ◽  
Author(s):  
JinE Li ◽  
ZhengYan Guo ◽  
Wei Huang ◽  
XiangXi Meng ◽  
GuoMin Ai ◽  
...  

ChemBioChem ◽  
2016 ◽  
Vol 17 (15) ◽  
pp. 1407-1411 ◽  
Author(s):  
Lihan Zhang ◽  
Shotaro Hoshino ◽  
Takayoshi Awakawa ◽  
Toshiyuki Wakimoto ◽  
Ikuro Abe

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