TY - JOUR
T1 - Structural Basis for Dynamic Interdomain Movement and RNA Recognition of the Selenocysteine-Specific Elongation Factor SelB
AU - Ose, Toyoyuki
AU - Soler, Nicolas
AU - Rasubala, Linda
AU - Kuroki, Kimiko
AU - Kohda, Daisuke
AU - Fourmy, Dominique
AU - Yoshizawa, Satoko
AU - Maenaka, Katsumi
N1 - Funding Information:
We thank M. Kawamoto, H. Sakai, N. Shimizu, K. Miura, and K. Hasegawa for assistance in data collection at SPring8. This work was supported by the joint program Japan Society for the Promotion of Science (JSPS)-Centre National de la Recherche Scientifique to S.Y. and K.M. and the French national program Geomicrobiologie des Environments Extremes (GEOMEX) to S.Y. and D.F. K.M. and D.K. were supported in part by Ministry of Education, Science, Sports, Culture and Technology of Japan and the Protein 3000 project. T.O. was supported by a JSPS postdoctoral fellowship and a Human Frontier Science Program long-term fellowship. L.R. was supported by a JSPS postdoctoral fellowship for foreign researchers.
PY - 2007/5/16
Y1 - 2007/5/16
N2 - Selenocysteine (Sec) is the "21st" amino acid and is genetically encoded by an unusual incorporation system. The stop codon UGA becomes a Sec codon when the selenocysteine insertion sequence (SECIS) exists downstream of UGA. Sec incorporation requires a specific elongation factor, SelB, which recognizes tRNASec via use of an EF-Tu-like domain and the SECIS mRNA hairpin via use of a C-terminal domain (SelB-C). SelB functions in multiple translational steps: binding to SECIS mRNA and tRNASec, delivery of tRNASec onto an A site, GTP hydrolysis, and release from tRNA and mRNA. However, this dynamic mechanism remains to be revealed. Here, we report a large domain rearrangement in the structure of SelB-C complexed with RNA. Surprisingly, the interdomain region forms new interactions with the phosphate backbone of a neighboring RNA, distinct from SECIS RNA binding. This SelB-RNA interaction is sequence independent, possibly reflecting SelB-tRNA/-rRNA recognitions. Based on these data, the dynamic SelB-ribosome-mRNA-tRNA interactions will be discussed.
AB - Selenocysteine (Sec) is the "21st" amino acid and is genetically encoded by an unusual incorporation system. The stop codon UGA becomes a Sec codon when the selenocysteine insertion sequence (SECIS) exists downstream of UGA. Sec incorporation requires a specific elongation factor, SelB, which recognizes tRNASec via use of an EF-Tu-like domain and the SECIS mRNA hairpin via use of a C-terminal domain (SelB-C). SelB functions in multiple translational steps: binding to SECIS mRNA and tRNASec, delivery of tRNASec onto an A site, GTP hydrolysis, and release from tRNA and mRNA. However, this dynamic mechanism remains to be revealed. Here, we report a large domain rearrangement in the structure of SelB-C complexed with RNA. Surprisingly, the interdomain region forms new interactions with the phosphate backbone of a neighboring RNA, distinct from SECIS RNA binding. This SelB-RNA interaction is sequence independent, possibly reflecting SelB-tRNA/-rRNA recognitions. Based on these data, the dynamic SelB-ribosome-mRNA-tRNA interactions will be discussed.
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U2 - 10.1016/j.str.2007.03.007
DO - 10.1016/j.str.2007.03.007
M3 - Article
C2 - 17502103
AN - SCOPUS:34248181181
SN - 0969-2126
VL - 15
SP - 577
EP - 586
JO - Structure
JF - Structure
IS - 5
ER -