Study of the TmoS TmoT two component system Towards the functional characterisation of the family of TodS TodT like systems
Yazarlar (6)
Prof. Dr. Bilge Hilal ÇADIRCI Tokat Gaziosmanpaşa Üniversitesi, Türkiye
| Makale Türü |
Özgün Makale
(SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
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| Dergi Adı | MICROBIAL BIOTECHNOLOGY (Q4) | ||
| Dergi ISSN | 1751-7907 | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 07-2012 |
| Cilt / Sayı / Sayfa | 5 / 4 / 489–500 | DOI | 10.1111/j.1751-7915.2011.00322.x |
| Makale Linki | https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1751-7915.2011.00322.x | ||
| Özet |
| The two‐component system TmoS/TmoT controls the expression of the toluene‐4‐monooxygenase pathway in Pseudomonas mendocina RK1 via modulation of PtmoX activity. The TmoS/TmoT system belongs to the family of TodS/TodT like proteins. The sensor kinase TmoS is a 108 kDa protein composed of seven different domains. Using isothermal titration calorimetry we show that purified TmoS binds a wide range of aromatic compounds with high affinities. Tightest ligand binding was observed for toluene (KD = 150 nM), which corresponds to the highest affinity measured between an effector and a sensor kinase. Other compounds with affinities in the nanomolar range include benzene, the 3 xylene isomers, styrene, nitrobenzene or p‐chlorotoluene. We demonstrate that only part of the ligands that bind to TmoS increase protein autophosphorylation in vitro and consequently pathway expression in vivo … |
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BM Sürdürülebilir Kalkınma Amaçları
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| WoS | 20 |
| SCOPUS | 20 |
| Google Scholar | 31 |