کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2030152 1071042 2006 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structural Basis for Sulfur Relay to RNA Mediated by Heterohexameric TusBCD Complex
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Structural Basis for Sulfur Relay to RNA Mediated by Heterohexameric TusBCD Complex
چکیده انگلیسی

SummaryUridine at wobble position 34 of tRNALys, tRNAGlu, and tRNAGln is exclusively modified into 2-thiouridine (s2U), which is crucial for both precise codon recognition and recognition by the cognate aminoacyl-tRNA synthetases. Recent Escherichia coli genetic studies revealed that the products of five novel genes, tusABCDE, function in the s2U modification. Here, we solved the 2.15 Å crystal structure of the E. coli TusBCD complex, a sulfur transfer mediator, forming a heterohexamer composed of a dimer of the heterotrimer. Structure-based sequence alignment suggested two putative active site Cys residues, Cys79 (in TusC) and Cys78 (in TusD), which are exposed on the hexameric complex. In vivo mutant analyses revealed that only Cys78, in the TusD subunit, participates in sulfur transfer during the s2U modification process. Since the single Cys acts as a catalytic residue, we proposed that TusBCD mediates sulfur relay via a putative persulfide state of the TusD subunit.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 14, Issue 2, 2 February 2006, Pages 357–366
نویسندگان
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