alexa Low Molecular Weight Protein Tyrosine Phosphatases Cont
ISSN: 2329-6674

Enzyme Engineering
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Research Article

Low Molecular Weight Protein Tyrosine Phosphatases Control Antibiotic Production in Streptomyces coelicolor A3(2)

Sujata Vijay Sohoni1,2, Sarah Lieder1,3, Prashant Bapat1,4, Ivan Mijakovic5 and Anna Eliasson Lantz1*
1Department of Systems Biology, Technical University of Denmark, Building 223, DK-2800 Kgs Lyngby, Denmark
2Department of Chemical Engineering, Indian Institute of Technology Bombay, Powai, Mumbai, 400076, India
3Institute of Biochemical Engineering, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany
4Novozymes A/S, Hallas Alle 1, 4400 Kalundborg, Denmark
5Systems Biology, Department of Chemical and Biological Engineering, Chalmers University of Technology, SE-41296 Gothenburg, Sweden
Corresponding Author : Anna Eliasson Lantz
Department of Systems Biology, Technical University of Denmark
Building 223, DK-2800 Kgs Lyngby, Denmark
Tel: +45-4525 2680
Fax: +45-4588 4148
E-mail: [email protected]
Received February 21, 2014; Accepted March 24, 2014; Published April 05, 2014
Citation: Sohoni SV, Lieder S, Bapat P, Mijakovic I, Lantz AE (2014) Low Molecular Weight Protein Tyrosine Phosphatases Control Antibiotic Production in Streptomyces coelicolor A3(2). Enz Eng 3:122. doi:10.4172/2329-6674.1000122
Copyright: © 2014 Sohoni SV, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


Streptomyces coelicolor A3(2) possesses a low molecular weight protein tyrosine phosphatase (LMW-PTP), PtpA, that affects the production of undecylprodigionsin (RED) and actinorhodin (ACT). In this study we identified another LMW-PTP called sco3700. Tyrosine phosphatase activity of the purified Sco3700 was established using para-nitrophenyl phosphate and the tyrosine-phosphorylated protein PtkA from Bacillus subtilis as substrates. The optimum pH for the Sco3700 phosphatase activity was 6.8, and KM for pNPP was 14.3 mM compared to pH 6.0 and KM0.75 mM for PtpA. The potential of Sco3700 to participate, alongside PtpA, in the regulation of S. coelicolor antibiotic production was investigated. Hence, S. coelicolor A3(2) strains with ptpA and sco3700 overexpression were constructed and characterized for growth, RED and ACT production. We did observe an increase in volumetric productivity of ACT in the ptpA over expression strain. Furthermore, a significantly earlier onset of ACT production was observed when ptpA was over expressed. Sco3700 overexpression had a pleiotropic effect on the cell, and the strain exhibited lower productivities and final concentrations of antibiotics. We conclude that Sco3700 is indeed a tyrosine phosphatase, and it contributes to regulation of antibiotic production in S. coelicolor affecting the timing of onset of the antibiotic production.


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