Characterization of a carboxylesterase with hyper-thermostability and alkali-stability from Streptomyces lividans TK24

Extremophiles ◽  
2021 ◽  
Author(s):  
Xin Chang ◽  
Shuang Wu ◽  
Jie Chen ◽  
Shengqi Xiong ◽  
Peng Wang ◽  
...  
Keyword(s):  
Streptomyces Lividans ◽  
Alkali Stability

scholarly journals Genetic and physiological characterization of rpoB mutations that activate antibiotic production in Streptomyces lividans

Microbiology ◽  
2002 ◽  
Vol 148 (11) ◽  
pp. 3365-3373 ◽  
Author(s):  
Caixia Lai ◽  
Jun Xu ◽  
Yuzuru Tozawa ◽  
Yoshiko Okamoto-Hosoya ◽  
Xingsheng Yao ◽  
...  
Keyword(s):  
Antibiotic Production ◽  
Streptomyces Lividans ◽  
Physiological Characterization

scholarly journals ʲ-mannanase of Streptomyces lividans 66: cloning and DNA sequence of the manA gene and characterization of the enzyme

1993 ◽  
Vol 290 (3) ◽  
pp. 857-863 ◽  
Author(s):  
N Arcand ◽  
D Kluepfel ◽  
F W Paradis ◽  
R Morosoli ◽  
F Shareck
Keyword(s):  
Dna Sequence ◽  
Wild Type Strain ◽  
Specific Activity ◽  
Streptomyces Lividans ◽  
Gene Coding ◽  
Sds Page ◽  
Main Carbon Source ◽  
Assay Conditions ◽  
Main Carbon

The gene coding for a beta-mannanase was cloned homologously from Streptomyces lividans and its DNA sequence was determined. The fully secreted enzyme was isolated and purified from culture filtrates of the hyperproducing clone S. lividans IAF36 grown in mineral salt media containing galactomannan as the main carbon source. It had a molecular mass of 36 kDa and a specific activity of 876 i.u./mg of protein. Under the assay conditions used, the optimal enzyme activity was obtained at 58 degrees C and a pH of 6.8. The pI was 3.5. The kinetic constants of this mannanase determined with galactomannan as substrate were a Vmax. of 205 i.u./mg of enzyme and a Km of 0.77 mg/ml. Data from SDS/PAGE and Western blotting show that the cloned enzyme was identical to that of the wild-type strain.

scholarly journals Characterization of Sigma Factor Genes in Streptomyces lividans TK24 Using a Genomic Library-Based Approach for Multiple Gene Deletions

2018 ◽  
Vol 9 ◽  
Author(s):  
Yuriy Rebets ◽  
Konstantinos C. Tsolis ◽  
Elísabet Eik Guðmundsdóttir ◽  
Joachim Koepff ◽  
Beata Wawiernia ◽  
...  
Keyword(s):  
Sigma Factor ◽  
Genomic Library ◽  
Streptomyces Lividans ◽  
Gene Deletions ◽  
Multiple Gene

scholarly journals Characterization of the Genetic Components of Streptomyces lividans Linear Plasmid SLP2 for Replication in Circular and Linear Modes

2006 ◽  
Vol 188 (19) ◽  
pp. 6851-6857 ◽  
Author(s):  
Mingxuan Xu ◽  
Yingmin Zhu ◽  
Ran Zhang ◽  
Meijuan Shen ◽  
Weihong Jiang ◽  
...  
Keyword(s):  
Streptomyces Lividans ◽  
Linear Plasmid ◽  
Replication Proteins ◽  
Linear Mode ◽  
Genetic Components ◽  
Efficient Replication ◽  
Telomere Replication ◽  
In Vitro Interactions

ABSTRACT The nucleotide sequence of Streptomyces lividans linear plasmid SLP2 consists of 50,410 bp (C. H. Huang, C. Y. Chen, H. H. Tsai, C. Chen, Y. S. Lin, and C. W. Chen, Mol. Microbiol. 47:1563-1576, 2003). Here we report that the basic SLP2 locus for plasmid replication in circular mode resembles that of Streptomyces linear plasmids pSLA2 and SCP1 and comprises iteronsSLP2 and the adjacent rep SLP2 gene. More efficient replication additionally required the 47-bp sequence between bp 581 and 628 upstream of the iterons. Replacement of either the iterons or the rep gene of SLP2 by the corresponding genes of pSLA2 or SCP1 still allows propagation in Streptomyces, although the transformation frequencies were 3 orders of magnitude lower than the original plasmids, suggesting that these plasmids share similar replication mechanisms. To replicate SLP2 in linear mode, additional SLP2 loci—either mtap SLP2 /tpg SLP2 or mtap SLP2 /ilrA SLP2 —were required. IlrASLP2 protein binds specifically to the iteronsSLP2 in vitro. Interactions were detected between these SLP2-borne replication proteins (MtapSLP2, TpgSLP2, and IlrASLP2) and the telomeric replication proteins (TpgL, TapL, and TpgL) of the S. lividans chromosome, respectively, but the SLP2 proteins failed to interact. These results suggest that SLP2 recruits chromosomally encoded replication proteins for its telomere replication.

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