کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2092521 1081796 2011 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A hybrid two-component system protein from Azospirillum brasilense Sp7 was involved in chemotaxis
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیوتکنولوژی یا زیست‌فناوری
پیش نمایش صفحه اول مقاله
A hybrid two-component system protein from Azospirillum brasilense Sp7 was involved in chemotaxis
چکیده انگلیسی

We here report the sequence and functional analysis of org35 of Azospirillum brasilense Sp7, which was originally identified to be able to interact with NifA in yeast-two-hybrid system. The org35 encodes a hybrid two-component system protein, including N-terminal PAS domains, a histidine kinase (HPK) domain and a response regulator (RR) domain in C-terminal. To determine the function of the Org35, a deletion–insertion mutant in PAS domain [named Sp7353] and a complemental strain Sp7353C were constructed. The mutant had reduced chemotaxis ability compared to that of wild-type, and the complemental strain was similar to the wild-type strain. These data suggested that the A. brasilense org35 played a key role in chemotaxis. Variants containing different domains of the org35 were expressed, and the functions of these domains were studied in vitro. Phosphorylation assays in vitro demonstrated that the HPK domain of Org35 possessed the autokinase activity and that the phosphorylated HPK was able to transfer phosphate groups to the RR domain. The result indicated Org35 was a phosphorylation-communicating protein.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Microbiological Research - Volume 166, Issue 6, 20 September 2011, Pages 458–467
نویسندگان
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