Knockout of N-hydroxybenzoate hydroxylase functional gene orf54 in Streptomyces sp. 13580 gene cluster and fermentation detection of its mutant strain

2019 ◽  
Author(s):  
Zhen Meng ◽  
Yunhua Hou
Keyword(s):  
Gene Cluster ◽  
Mutant Strain ◽  
Functional Gene ◽  
Streptomyces Sp ◽  
Hydroxybenzoate Hydroxylase

Identification of the kinanthraquinone biosynthetic gene cluster by expression of an atypical response regulator

2021 ◽  
Vol 85 (3) ◽  
pp. 714-721
Author(s):  
Risa Takao ◽  
Katsuyuki Sakai ◽  
Hiroyuki Koshino ◽  
Hiroyuki Osada ◽  
Shunji Takahashi
Keyword(s):  
Heterologous Expression ◽  
Gene Cluster ◽  
Secondary Metabolite ◽  
Response Regulator ◽  
Bac Library ◽  
Gene Clusters ◽  
Biosynthetic Gene Cluster ◽  
Gene Organization ◽  
Biosynthetic Gene ◽  
Streptomyces Sp

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.

scholarly journals Mining of a streptothricin gene cluster from Streptomyces sp. TP-A0356 genome via heterologous expression

2013 ◽  
Vol 56 (7) ◽  
pp. 619-627 ◽  
Author(s):  
JinE Li ◽  
ZhengYan Guo ◽  
Wei Huang ◽  
XiangXi Meng ◽  
GuoMin Ai ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Gene Cluster ◽  
Streptomyces Sp

scholarly journals Anthracycline metabolites from baumycin-producing Streptomyces sp. D788. II. New anthracycline metabolites produced by a blocked mutant strain RPM-5.

1993 ◽  
Vol 46 (1) ◽  
pp. 56-64 ◽  
Author(s):  
AKIHIRO YOSHIMOTO ◽  
SHIZUKA FUJII ◽  
OSAMU JOHDO ◽  
KATSURO KUBO ◽  
HIROSHI NISHIDA ◽  
...  
Keyword(s):  
Mutant Strain ◽  
Streptomyces Sp

Isolation and characterization of meridamycin biosynthetic gene cluster from Streptomyces sp. NRRL 30748

Gene ◽  
2006 ◽  
Vol 377 ◽  
pp. 109-118 ◽  
Author(s):  
Min He ◽  
Bradley Haltli ◽  
Mia Summers ◽  
Xidong Feng ◽  
John Hucul
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Gene Cluster ◽  
Biosynthetic Gene ◽  
Streptomyces Sp ◽  
Isolation And Characterization

Activation and Characterization of Bohemamine Biosynthetic Gene Cluster from Streptomyces sp. CB02009

2020 ◽  
Vol 22 (12) ◽  
pp. 4614-4619 ◽  
Author(s):  
Ling Liu ◽  
Sainan Li ◽  
Runze Sun ◽  
Xiangjing Qin ◽  
Jianhua Ju ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Gene Cluster ◽  
Biosynthetic Gene ◽  
Streptomyces Sp

scholarly journals Partial Activation of a Silent Angucycline-type Gene Cluster from a Rubromycin .BETA. Producing Streptomyces sp. PGA64

2004 ◽  
Vol 57 (8) ◽  
pp. 502-510 ◽  
Author(s):  
MIKKO METSÄ-KETELÄ ◽  
KRISTIINA YLIHONKO ◽  
PEKKA MÄNTSÄLÄ
Keyword(s):  
Gene Cluster ◽  
Streptomyces Sp ◽  
Partial Activation ◽  
Type Gene

scholarly journals Gene Cluster Involved in the Biosynthesis of Griseobactin, a Catechol-Peptide Siderophore of Streptomyces sp. ATCC 700974

2009 ◽  
Vol 192 (2) ◽  
pp. 426-435 ◽  
Author(s):  
Silke I. Patzer ◽  
Volkmar Braun
Keyword(s):  
Gene Cluster ◽  
Linear Form ◽  
Streptomyces Griseus ◽  
Biosynthetic Gene Cluster ◽  
Peptide Structure ◽  
Biosynthetic Gene ◽  
Biosynthesis Gene Cluster ◽  
Streptomyces Sp ◽  
Peptide Synthetase ◽  
Biosynthesis Gene

ABSTRACT The main siderophores produced by streptomycetes are desferrioxamines. Here we show that Streptomyces sp. ATCC 700974 and several Streptomyces griseus strains, in addition, synthesize a hitherto unknown siderophore with a catechol-peptide structure, named griseobactin. The production is repressed by iron. We sequenced a 26-kb DNA region comprising a siderophore biosynthetic gene cluster encoding proteins similar to DhbABCEFG, which are involved in the biosynthesis of 2,3-dihydroxybenzoate (DHBA) and in the incorporation of DHBA into siderophores via a nonribosomal peptide synthetase. Adjacent to the biosynthesis genes are genes that encode proteins for the secretion, uptake, and degradation of siderophores. To correlate the gene cluster with griseobactin synthesis, the dhb genes in ATCC 700974 were disrupted. The resulting mutants no longer synthesized DHBA and griseobactin; production of both was restored by complementation with the dhb genes. Heterologous expression of the dhb genes or of the entire griseobactin biosynthesis gene cluster in the catechol-negative strain Streptomyces lividans TK23 resulted in the synthesis and secretion of DHBA or griseobactin, respectively, suggesting that these genes are sufficient for DHBA and griseobactin biosynthesis. Griseobactin was purified and characterized; its structure is consistent with a cyclic and, to a lesser extent, linear form of the trimeric ester of 2,3-dihydroxybenzoyl-arginyl-threonine complexed with aluminum under iron-limiting conditions. This is the first report identifying the gene cluster for the biosynthesis of DHBA and a catechol siderophore in Streptomyces.

scholarly journals Involvement of the XpsN Protein in Formation of the XpsL-XpsM Complex in Xanthomonas campestris pv. campestris Type II Secretion Apparatus

2001 ◽  
Vol 183 (2) ◽  
pp. 528-535 ◽  
Author(s):  
Hsien-Ming Lee ◽  
Shiaw-Wei Tyan ◽  
Wei-Ming Leu ◽  
Ling-Yun Chen ◽  
David Chanhen Chen ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Mutant Strain ◽  
Type Strain ◽  
Xanthomonas Campestris ◽  
Wild Type Strain ◽  
Type Ii ◽  
Wild Type ◽  
In The Wild ◽  
Steady State Levels ◽  
Type Gene

ABSTRACT The xps gene cluster is required for the second step of type II protein secretion in Xanthomonas campestrispv. campestris. Deletion of the entire gene cluster caused accumulation of secreted proteins in the periplasm. By analyzing protein abundance in the chromosomal mutant strains, we observed mutual dependence for normal steady-state levels between the XpsL and the XpsM proteins. The XpsL protein was undetectable in total lysate prepared from thexpsM mutant strain, and vice versa. Introduction of the wild-type xpsM gene carried on a plasmid into thexpsM mutant strain was sufficient for reappearance of the XpsL protein, and vice versa. Moreover, both XpsL and XpsM proteins were undetectable in the xpsN mutant strain. They were recovered either by reintroducing the wild-type xpsNgene or by introducing extra copies of wild-type xpsL orxpsM individually. Overproduction of wild-type XpsL and -M proteins simultaneously, but not separately, in the wild-type strain of X. campestris pv. campestris caused inhibition of secretion. Complementation of an xpsL orxpsM mutant strain with a plasmid-borne wild-type gene was inhibited by coexpression of XpsL and XpsM. The presence of the xpsN gene on the plasmid along with thexpsL and the xpsM genes caused more severe inhibition in both cases. Furthermore, complementation of thexpsN mutant strain was also inhibited. In both the wild-type strain and a strain with the xps gene cluster deleted (XC17433), carrying pCPP-LMN, which encodes all three proteins, each protein coprecipitated with the other two upon immunoprecipitation. Expression of pairwise combinations of the three proteins in XC17433 revealed that the XpsL-XpsM and XpsM-XpsN pairs still coprecipitated, whereas the XpsL-XpsN pair no longer coprecipitated.

Sign in / Sign up

Export Citation Format

Share Document