کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
7560878 1491448 2013 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners
چکیده انگلیسی
The TTSS is used by Salmonella and many bacterial pathogens to inject virulence factors directly into the cytoplasm of target eukaryotic cells. Once translocated these so-called effector proteins hijack a vast array of crucial cellular functions to the benefit of the bacteria. In the bacterial cytoplasm, some effectors are stabilized and maintained in a secretion competent state by interaction with specific type III chaperones. In this work we studied the conformation of the Chaperone Binding Domain of the effector named Salmonella Outer protein B (SopB) alone and in complex with its cognate chaperone SigE by a combination of biochemical, biophysical and structural approaches. Our results show that the N-terminus part of SopB is mainly composed by α-helices and unfolded regions whose organization/stabilization depends on their interaction with the different partners. This suggests that the partially unfolded state of this N-terminal region, which confers the adaptability of the effector to bind very different partners during the infection cycle, allows the bacteria to modulate numerous host cells functions limiting the number of translocated effectors.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1834, Issue 12, December 2013, Pages 2564-2572
نویسندگان
, , , , , , , , ,