Structural characterization of the intra-membrane histidine kinase YbdK from Bacillus subtilis in DPC micelles
- Division of Magnetic Resonance, Korea Basic Science Institute (KBSI), 804-1, Yangcheong-Ri, Ochang, Chungbuk 363-883 (Korea, Republic of)
- Systems Microbiology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), 52, Eoeun-Dong, Yuseong-Gu, Daejeon 305-333 (Korea, Republic of)
- School of Life Sciences, Chungbuk National University, Cheongju 361-763 (Korea, Republic of)
Bacterial histidine kinases (HKs) play a critical role in signal transduction for cellular adaptation to environmental conditions and stresses. YbdK from Bacillus subtilis is a 320-residue intra-membrane sensing HK characterized by a short input domain consisting of two transmembrane helices without an extracytoplasmic domain. While the cytoplasmic domains of HKs have been studied in detail, the intra-membrane sensing domain systems are still uncharacterized due to difficulties in handling the transmembrane domain. Here, we successfully obtained pure recombinant transmembrane domain of YbdK (YbdK-TM) from E. coli and analyzed the characteristics of YbdK-TM using nuclear magnetic resonance (NMR) and other biophysical methods. YbdK-TM was found to form homo-dimers in DPC micelles based on cross-linking assays and analytical ultracentrifugation analyses. We estimated the size of the YbdK-TM DPC complex to be 46 kDa using solution state NMR T{sub 1}/T{sub 2} relaxation analyses in DPC micelles. These results provide information that will allow functional and structural studies of intra-membrane sensing HKs to begin.
- OSTI ID:
- 22202333
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 391, Issue 3; Other Information: Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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