Structural characterization of the intra-membrane histidine kinase YbdK from Bacillus subtilis in DPC micelles

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Title
Structural characterization of the intra-membrane histidine kinase YbdK from Bacillus subtilis in DPC micelles
Author(s)
Y P Kim; K J Yeo; Myung Hee Kim; Y C Kim; Y H Jeon
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 391, no. 3, pp. 1506-1511
Publication Year
2010
Abstract
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 T1/T2 relaxation analyses in DPC micelles. These results provide information that will allow functional and structural studies of intra-membrane sensing HKs to begin.
Keyword
DimerHistidine kinaseIntra-membrane sensing histidine kinaseTransmembrane proteinYbdk
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2009.12.106
Type
Article
Appears in Collections:
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
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