کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1932538 1050584 2010 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structural characterization of the intra-membrane histidine kinase YbdK from Bacillus subtilis in DPC micelles
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Structural characterization of the intra-membrane histidine kinase YbdK from Bacillus subtilis in DPC micelles
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 391, Issue 3, 15 January 2010, Pages 1506–1511
نویسندگان
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