کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1937299 | 1050713 | 2007 | 6 صفحه PDF | دانلود رایگان |
Escherichia coli MutS, an 853 amino acids oligomeric protein, is involved in the postreplicative DNA mismatch repair and avoidance of homeologous recombination. By constructing MutS mutated versions of the C-terminal region, we determined that deletion of the last 7 C-terminal amino acids is enough to abolish tetramer formation and that the K850A substitution destabilize the tetramer structure. It is proposed that the C-terminal extreme alpha helix (residues 839–850) of the protein may play an important role in protein oligomerization. We also show that the C-terminal region or the C-terminal plus the HTH domain of MutS, fused to the monomeric Maltose Binding Protein promote oligomerization of the chimeric protein. However, chemical cross-linking experiments indicate that the HTH domain improves the oligomerization properties of the fused protein. Escherichia coli cells expressing the fused proteins become hypermutator suggesting that the C-terminal region of MutS plays an important role in vivo.
Journal: Biochemical and Biophysical Research Communications - Volume 360, Issue 2, 24 August 2007, Pages 412–417