Identification of a conserved DNA sulfur recognition domain by characterizing the phosphorothioate-specific endonuclease SprMcrA from Streptomyces pristinaespiralis

2018 ◽  
Vol 110 (3) ◽  
pp. 484-497 ◽  
Author(s):  
Hao Yu ◽  
Guang Liu ◽  
Gong Zhao ◽  
Wenyue Hu ◽  
Geng Wu ◽  
...  
1997 ◽  
Vol 41 (9) ◽  
pp. 1904-1909 ◽  
Author(s):  
V de Crécy-Lagard ◽  
W Saurin ◽  
D Thibaut ◽  
P Gil ◽  
L Naudin ◽  
...  

Streptomyces pristinaespiralis and S. virginiae both produce closely related hexadepsipeptide antibiotics of the streptogramin B family. Pristinamycins I and virginiamycins S differ only in the fifth incorporated precursor, di(mono)methylated amine and phenylalanine, respectively. By using degenerate oligonucleotide probes derived from internal sequences of the purified S. pristinaespiralis SnbD and SnbE proteins, the genes from two streptogramin B producers, S. pristinaespiralis and S. virginiae, encoding the peptide synthetase involved in the activation and incorporation of the last four precursors (proline, 4-dimethylparaaminophenylalanine [for pristinamycin I(A)] or phenylalanine [for virginiamycin S], pipecolic acid, and phenylglycine) were cloned. Analysis of the sequence revealed that SnbD and SnbE are encoded by a unique snbDE gene. SnbDE (4,849 amino acids [aa]) contains four amino acid activation domains, four condensation domains, an N-methylation domain, and a C-terminal thioesterase domain. Comparison of the sequences of 55 amino acid-activating modules from different origins confirmed that these sequences contain enough information for the performance of legitimate predictions of their substrate specificity. Partial sequencing (1,993 aa) of the SnbDE protein of S. virginiae allowed comparison of the proline and aromatic acid activation domains of the two species and the identification of coupled frameshift mutations.


2015 ◽  
Vol 49 (2) ◽  
pp. 253-259
Author(s):  
Q. -C. Jin ◽  
N. Shen ◽  
H. Yin ◽  
Y. Yang ◽  
Z. -H. Jin

2007 ◽  
Vol 42 (4) ◽  
pp. 700-703 ◽  
Author(s):  
Maxime Limonet ◽  
Sophie Saffroy ◽  
Frédéric Maujean ◽  
Michel Linder ◽  
Stéphane Delaunay

2015 ◽  
Vol 81 (19) ◽  
pp. 6621-6636 ◽  
Author(s):  
Yvonne Mast ◽  
Jamil Guezguez ◽  
Franziska Handel ◽  
Eva Schinko

ABSTRACTPristinamycin production inStreptomyces pristinaespiralisPr11 is tightly regulated by an interplay between different repressors and activators. A γ-butyrolactone receptor gene (spbR), two TetR repressor genes (papR3andpapR5), three SARP (Streptomycesantibioticregulatoryprotein) genes (papR1,papR2, andpapR4), and a response regulator gene (papR6) are carried on the large 210-kb pristinamycin biosynthetic gene region ofStreptomyces pristinaespiralisPr11. A detailed investigation of all pristinamycin regulators revealed insight into a complex signaling cascade, which is responsible for the fine-tuned regulation of pristinamycin production inS. pristinaespiralis.


2010 ◽  
Vol 4 (2) ◽  
pp. 192-206 ◽  
Author(s):  
Yvonne Mast ◽  
Tilmann Weber ◽  
Melanie Gölz ◽  
Regina Ort-Winklbauer ◽  
Anne Gondran ◽  
...  

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