Structural basis of RNA-dependent recruitment of glutamine to the genetic code
Glutaminyl-transfer RNA (Gln-tRNA(Gln)) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNA(Gln) by the heterodimeric Glu-tRNA(Gln) amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNA(Gln) at...
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| Vydáno v: | Science (American Association for the Advancement of Science) Ročník 312; číslo 5782; s. 1950 |
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| Médium: | Journal Article |
| Jazyk: | angličtina |
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United States
30.06.2006
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| ISSN: | 1095-9203, 1095-9203 |
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| Abstract | Glutaminyl-transfer RNA (Gln-tRNA(Gln)) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNA(Gln) by the heterodimeric Glu-tRNA(Gln) amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNA(Gln) at 3.15 angstroms resolution. Biochemical analysis of GatDE and of tRNA(Gln) mutants characterized the catalytic centers for the enzyme's three reactions (glutaminase, kinase, and amidotransferase activity). A 40 angstrom-long channel for ammonia transport connects the active sites in GatD and GatE. tRNA(Gln) recognition by indirect readout based on shape complementarity of the D loop suggests an early anticodon-independent RNA-based mechanism for adding glutamine to the genetic code. |
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| AbstractList | Glutaminyl-transfer RNA (Gln-tRNA(Gln)) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNA(Gln) by the heterodimeric Glu-tRNA(Gln) amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNA(Gln) at 3.15 angstroms resolution. Biochemical analysis of GatDE and of tRNA(Gln) mutants characterized the catalytic centers for the enzyme's three reactions (glutaminase, kinase, and amidotransferase activity). A 40 angstrom-long channel for ammonia transport connects the active sites in GatD and GatE. tRNA(Gln) recognition by indirect readout based on shape complementarity of the D loop suggests an early anticodon-independent RNA-based mechanism for adding glutamine to the genetic code.Glutaminyl-transfer RNA (Gln-tRNA(Gln)) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNA(Gln) by the heterodimeric Glu-tRNA(Gln) amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNA(Gln) at 3.15 angstroms resolution. Biochemical analysis of GatDE and of tRNA(Gln) mutants characterized the catalytic centers for the enzyme's three reactions (glutaminase, kinase, and amidotransferase activity). A 40 angstrom-long channel for ammonia transport connects the active sites in GatD and GatE. tRNA(Gln) recognition by indirect readout based on shape complementarity of the D loop suggests an early anticodon-independent RNA-based mechanism for adding glutamine to the genetic code. Glutaminyl-transfer RNA (Gln-tRNA(Gln)) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNA(Gln) by the heterodimeric Glu-tRNA(Gln) amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNA(Gln) at 3.15 angstroms resolution. Biochemical analysis of GatDE and of tRNA(Gln) mutants characterized the catalytic centers for the enzyme's three reactions (glutaminase, kinase, and amidotransferase activity). A 40 angstrom-long channel for ammonia transport connects the active sites in GatD and GatE. tRNA(Gln) recognition by indirect readout based on shape complementarity of the D loop suggests an early anticodon-independent RNA-based mechanism for adding glutamine to the genetic code. |
| Author | Feng, Liang Nakamura, Yuko Blanquet, Sylvain Nureki, Osamu Sherrer, R Lynn Schmitt, Emmanuelle Söll, Dieter Ishitani, Ryuichiro Mechulam, Yves Oshikane, Hiroyuki Fukai, Shuya Panvert, Michel Sheppard, Kelly Numata, Tomoyuki |
| Author_xml | – sequence: 1 givenname: Hiroyuki surname: Oshikane fullname: Oshikane, Hiroyuki organization: Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan – sequence: 2 givenname: Kelly surname: Sheppard fullname: Sheppard, Kelly – sequence: 3 givenname: Shuya surname: Fukai fullname: Fukai, Shuya – sequence: 4 givenname: Yuko surname: Nakamura fullname: Nakamura, Yuko – sequence: 5 givenname: Ryuichiro surname: Ishitani fullname: Ishitani, Ryuichiro – sequence: 6 givenname: Tomoyuki surname: Numata fullname: Numata, Tomoyuki – sequence: 7 givenname: R Lynn surname: Sherrer fullname: Sherrer, R Lynn – sequence: 8 givenname: Liang surname: Feng fullname: Feng, Liang – sequence: 9 givenname: Emmanuelle surname: Schmitt fullname: Schmitt, Emmanuelle – sequence: 10 givenname: Michel surname: Panvert fullname: Panvert, Michel – sequence: 11 givenname: Sylvain surname: Blanquet fullname: Blanquet, Sylvain – sequence: 12 givenname: Yves surname: Mechulam fullname: Mechulam, Yves – sequence: 13 givenname: Dieter surname: Söll fullname: Söll, Dieter – sequence: 14 givenname: Osamu surname: Nureki fullname: Nureki, Osamu |
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| Snippet | Glutaminyl-transfer RNA (Gln-tRNA(Gln)) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNA(Gln) by the heterodimeric... |
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| SubjectTerms | Acylation Adenosine Triphosphate - metabolism Ammonia - metabolism Anticodon Binding Sites Catalytic Domain Computer Simulation Crystallography, X-Ray Dimerization Genetic Code Glutamine - metabolism Hydrogen Bonding Magnesium - metabolism Methanobacteriaceae - enzymology Methanobacteriaceae - genetics Models, Molecular Mutation Nitrogenous Group Transferases - chemistry Nitrogenous Group Transferases - metabolism Nucleic Acid Conformation Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary RNA, Archaeal - chemistry RNA, Archaeal - metabolism RNA, Transfer, Gln - chemistry RNA, Transfer, Gln - metabolism |
| Title | Structural basis of RNA-dependent recruitment of glutamine to the genetic code |
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