Study of the TmoS TmoT two component system Towards the functional characterisation of the family of TodS TodT like systems
Yazarlar (6)
Silva-Jimenez Hortencia
Garcia-Fontana Cristina
Prof. Dr. Bilge Hilal ÇADIRCI Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Ramos-Gonzalez Maria Isabel
Juan Luis Ramos
Krell Tino
| 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 |
| Kabul Tarihi | – | Yayınlanma Tarihi | 27-12-2011 |
| Cilt / Sayı / Sayfa | 5 / 4 / 489–500 | DOI | 10.1111/j.1751-7915.2011.00322.x |
| Makale Linki | http://www.ncbi.nlm.nih.gov/pubmed/22212183 | ||
| UAK Araştırma Alanları |
Mikrobiyoloji
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| 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 … |
| Anahtar Kelimeler |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| Web of Science | 20 |
| Google Scholar | 31 |