TY - JOUR
T1 - Structural basis for sulfur relay to RNA mediated by heterohexameric TusBCD complex
AU - Numata, Tomoyuki
AU - Fukai, Shuya
AU - Ikeuchi, Yoshiho
AU - Suzuki, Tsutomu
AU - Nureki, Osamu
N1 - Funding Information:
We thank M. Kawamoto and N. Shimizu (Japan Synchrotron Radiation Research Institute) for their help in data collection at SPring-8. This work was supported by a grant from the Ministry of Education, Culture, Sports, Science and Technology to O.N. and T.S., by a Japan Society for the Promotion of Science Fellowship for Japanese Junior Scientists to Y.I., and by a Precursory Research for Embryonic Science and Technology Program grant from JST (Japan Science and Technology), and Sumitomo and Naito Foundation grants to O.N.
PY - 2006/2
Y1 - 2006/2
N2 - Uridine at wobble position 34 of tRNALys, tRNAGlu, and tRNAGln is exclusively modified into 2-thiouridine (s 2U), 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.
AB - Uridine at wobble position 34 of tRNALys, tRNAGlu, and tRNAGln is exclusively modified into 2-thiouridine (s 2U), 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.
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U2 - 10.1016/j.str.2005.11.009
DO - 10.1016/j.str.2005.11.009
M3 - Article
C2 - 16472754
AN - SCOPUS:32044441001
VL - 14
SP - 357
EP - 366
JO - Structure with Folding & design
JF - Structure with Folding & design
SN - 0969-2126
IS - 2
ER -