کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9882078 | 1536536 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
ClpB and DnaK form a bi-chaperone system that reactivates strongly aggregated proteins in vivo and in vitro. Previously observed interaction between purified ClpB and DnaK suggested that one of the chaperones might recruit its partner during substrate reactivation. We show that ClpB from Escherichia coli binds at the substrate binding site of DnaK and the interaction is supported by the N-terminal domain and the middle domain of ClpB. Moreover, the interaction between ClpB and DnaK depends on the nucleotide-state of DnaK: it is stimulated by ADP and inhibited by ATP. These observations indicate that DnaK recognizes selected structural motifs in ClpB as “pseudo-substrates” and that ClpB may compete with bona fide substrates of DnaK. We conclude that direct interaction between ClpB and DnaK does not mediate a substrate transfer between the chaperones, it may, however, play a role in the recruitment of the bi-chaperone system to specific recognition sites in aggregated particles.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 444, Issue 1, 1 December 2005, Pages 61-65
Journal: Archives of Biochemistry and Biophysics - Volume 444, Issue 1, 1 December 2005, Pages 61-65
نویسندگان
Sabina Kedzierska, Liudmila S. Chesnokova, Stephan N. Witt, Michal Zolkiewski,