The mtaA Gene of the Myxothiazol Biosynthetic Gene Cluster from Stigmatella aurantiaca DW4/3-1 Encodes a Phosphopantetheinyl Transferase that Activates Polyketide Synthases and Polypeptide Synthetases

2001 ◽  
Vol 129 (1) ◽  
pp. 119-124 ◽  
Author(s):  
N. Gaitatzis ◽  
A. Hans ◽  
R. Muller ◽  
S. Beyer
2005 ◽  
Vol 12 (3) ◽  
pp. 293-302 ◽  
Author(s):  
Wen Liu ◽  
Koichi Nonaka ◽  
Liping Nie ◽  
Jian Zhang ◽  
Steven D. Christenson ◽  
...  

2014 ◽  
Vol 58 (12) ◽  
pp. 7441-7450 ◽  
Author(s):  
Lorena T. Fernández-Martínez ◽  
Chiara Borsetto ◽  
Juan Pablo Gomez-Escribano ◽  
Maureen J. Bibb ◽  
Mahmoud M. Al-Bassam ◽  
...  

ABSTRACTComparative genome analysis revealed seven uncharacterized genes,sven0909tosven0915, adjacent to the previously identified chloramphenicol biosynthetic gene cluster (sven0916–sven0928) ofStreptomyces venezuelaestrain ATCC 10712 that was absent in a closely relatedStreptomycesstrain that does not produce chloramphenicol. Transcriptional analysis suggested that three of these genes might be involved in chloramphenicol production, a prediction confirmed by the construction of deletion mutants. These three genes encode a cluster-associated transcriptional activator (Sven0913), a phosphopantetheinyl transferase (Sven0914), and a Na+/H+antiporter (Sven0915). Bioinformatic analysis also revealed the presence of a previously undetected gene,sven0925, embedded within the chloramphenicol biosynthetic gene cluster that appears to encode an acyl carrier protein, bringing the number of new genes likely to be involved in chloramphenicol production to four. Microarray experiments and synteny comparisons also suggest thatsven0929is part of the biosynthetic gene cluster. This has allowed us to propose an updated and revised version of the chloramphenicol biosynthetic pathway.


2006 ◽  
Vol 72 (12) ◽  
pp. 7485-7494 ◽  
Author(s):  
Olena Perlova ◽  
Jun Fu ◽  
Silvia Kuhlmann ◽  
Daniel Krug ◽  
A. Francis Stewart ◽  
...  

ABSTRACT Although many secondary metabolites exhibiting important pharmaceutical and agrochemical activities have been isolated from myxobacteria, most of these microorganisms remain difficult to handle genetically. To utilize their metabolic potential, heterologous expression methodologies are currently being developed. Here, the Red/ET recombination technology was used to perform all required gene cluster engineering steps in Escherichia coli prior to the transfer into the chromosome of the heterologous host. We describe the integration of the complete 57-kbp myxothiazol biosynthetic gene cluster reconstituted from two cosmids from a cosmid library of the myxobacterium Stigmatella aurantiaca DW4-3/1 into the chromosome of the thus far best-characterized myxobacterium, Myxococcus xanthus, in one step. The successful integration and expression of the myxothiazol biosynthetic genes in M. xanthus results in the production of myxothiazol in yields comparable to the natural producer strain.


Author(s):  
Joana Martins ◽  
Niina Leikoski ◽  
Matti Wahlsten ◽  
Joana Azevedo ◽  
Jorge Antunes ◽  
...  

Cyanobactins are a family of linear and cyclic peptides produced through the post-translational modification of short precursor peptides. Anacyclamides are macrocyclic cyanobactins with a highly diverse sequence that are common in the genus <i>Anabaena</i>. A mass spectrometry-based screening of potential cyanobactin producers led to the discovery of a new prenylated member of this family of compounds, anacyclamide D8P (<b>1</b>), from <i>Sphaerospermopsis</i> sp. LEGE 00249. The anacyclamide biosynthetic gene cluster (<i>acy</i>) encoding the novel macrocyclic prenylated cyanobactin, was sequenced. Heterologous expression of the acy gene cluster in <i>Escherichia</i> <i>coli</i> established the connection between genomic and mass spectrometric data. Unambiguous establishment of the type and site of prenylation required the full structural elucidation of <b>1</b> using Nuclear Magnetic Resonance (NMR), which demonstrated that a forward prenylation occurred on the tyrosine residue. Compound <b>1</b> was tested in pharmacologically or ecologically relevant biological assays and revealed moderate antimicrobial activity towards the fouling bacterium <i>Halomonas aquamarina</i> CECT 5000.<br>


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