Structural basis of RNA-dependent recruitment of glutamine to the genetic code

Hiroyuki Oshikane; Kelly Sheppard; Shuya Fukai; Yuko Nakamura; Ryuichiro Ishitani; Tomoyuki Numata; R. Lynn Sherrer; Liang Feng; Emmanuelle Schmitt; Michel Panvert; Sylvain Blanquet; Yves Mechulam; Dieter Söll; Osamu Nureki

doi:10.1126/science.1128470

Structural basis of RNA-dependent recruitment of glutamine to the genetic code

Hiroyuki Oshikane
, Kelly Sheppard
, Shuya Fukai
, Yuko Nakamura
, Ryuichiro Ishitani
, Tomoyuki Numata
, R. Lynn Sherrer
, Liang Feng
, Emmanuelle Schmitt
, Michel Panvert
, Sylvain Blanquet
, Yves Mechulam
, Dieter Söll
, Osamu Nureki

Résultats de recherche: Contribution à un journal › Article › Revue par des pairs

Résumé

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 antkodon-independent RNA-based mechanism for adding glutamine to the genetic code.

langue originale	Anglais
Pages (de - à)	1950-1954
Nombre de pages	5
journal	Science
Volume	312
Numéro de publication	5782
Les DOIs	https://doi.org/10.1126/science.1128470
état	Publié - 30 juin 2006

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10.1126/science.1128470

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@article{43929794b5cf451b9a238639841cc91a,

title = "Structural basis of RNA-dependent recruitment of glutamine to the genetic code",

abstract = "Glutaminyl-transfer RNA (Gln-tRNAGln) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNAGln by the heterodimeric Glu-tRNAGln amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNAGln at 3.15 angstroms resolution. Biochemical analysis of GatDE and of tRNAGln 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. tRNAGln recognition by indirect readout based on shape complementarity of the D loop suggests an early antkodon-independent RNA-based mechanism for adding glutamine to the genetic code.",

author = "Hiroyuki Oshikane and Kelly Sheppard and Shuya Fukai and Yuko Nakamura and Ryuichiro Ishitani and Tomoyuki Numata and Sherrer, \{R. Lynn\} and Liang Feng and Emmanuelle Schmitt and Michel Panvert and Sylvain Blanquet and Yves Mechulam and Dieter S{\"o}ll and Osamu Nureki",

year = "2006",

month = jun,

day = "30",

doi = "10.1126/science.1128470",

language = "English",

volume = "312",

pages = "1950--1954",

journal = "Science",

issn = "0036-8075",

number = "5782",

}

TY - JOUR

T1 - Structural basis of RNA-dependent recruitment of glutamine to the genetic code

AU - Oshikane, Hiroyuki

AU - Sheppard, Kelly

AU - Fukai, Shuya

AU - Nakamura, Yuko

AU - Ishitani, Ryuichiro

AU - Numata, Tomoyuki

AU - Sherrer, R. Lynn

AU - Feng, Liang

AU - Schmitt, Emmanuelle

AU - Panvert, Michel

AU - Blanquet, Sylvain

AU - Mechulam, Yves

AU - Söll, Dieter

AU - Nureki, Osamu

PY - 2006/6/30

Y1 - 2006/6/30

N2 - Glutaminyl-transfer RNA (Gln-tRNAGln) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNAGln by the heterodimeric Glu-tRNAGln amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNAGln at 3.15 angstroms resolution. Biochemical analysis of GatDE and of tRNAGln 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. tRNAGln recognition by indirect readout based on shape complementarity of the D loop suggests an early antkodon-independent RNA-based mechanism for adding glutamine to the genetic code.

AB - Glutaminyl-transfer RNA (Gln-tRNAGln) in archaea is synthesized in a pretranslational amidation of misacylated Glu-tRNAGln by the heterodimeric Glu-tRNAGln amidotransferase GatDE. Here we report the crystal structure of the Methanothermobacter thermautotrophicus GatDE complexed to tRNAGln at 3.15 angstroms resolution. Biochemical analysis of GatDE and of tRNAGln 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. tRNAGln recognition by indirect readout based on shape complementarity of the D loop suggests an early antkodon-independent RNA-based mechanism for adding glutamine to the genetic code.

UR - https://www.scopus.com/pages/publications/33745587780

U2 - 10.1126/science.1128470

DO - 10.1126/science.1128470

M3 - Article

C2 - 16809540

AN - SCOPUS:33745587780

SN - 0036-8075

VL - 312

SP - 1950

EP - 1954

JO - Science

JF - Science

IS - 5782

ER -

Structural basis of RNA-dependent recruitment of glutamine to the genetic code

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