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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/16286
Title: Dual-mode recognition of noncanonical tRNAs<sup>Ser</sup> by seryl-tRNA synthetase in mammalian mitochondria
Authors: Sarin Chimnaronk
Mads Gravers Jeppesen
Tsutomu Suzuki
Jens Nyborg
Kimitsuna Watanabe
University of Tokyo
Aarhus Universitet
National Institute of Advanced Industrial Science and Technology
Mahidol University
Hokkaido University
Keywords: Biochemistry, Genetics and Molecular Biology;Immunology and Microbiology;Neuroscience
Issue Date: 5-Oct-2005
Citation: EMBO Journal. Vol.24, No.19 (2005), 3369-3379
Abstract: The secondary structures of metazoan mitochondrial (mt) tRNAsSer deviate markedly from the paradigm of the canonical cloverleaf structure; particularly, tRNASerGCU corresponding to the AGY codon (Y=U and C) is highly truncated and intrinsically missing the entire dihydrouridine arm. None of the mt serine isoacceptors possesses the elongated variable arm, which is the universal landmark for recognition by seryl-tRNA synthetase (SerRS). Here, we report the crystal structure of mammalian mt SerRS from Bos taurus in complex with seryl adenylate at an atomic resolution of 1.65 Å. Coupling structural information with a tRNA-docking model and the mutagenesis studies, we have unraveled the key elements that establish tRNA binding specificity, differ from all other known bacterial and eukaryotic systems, are the characteristic extensions in both extremities, as well as a few basic residues residing in the amino-terminal helical arm of mt SerRS. Our data further uncover an unprecedented mechanism of a dual-mode recognition employed to discriminate two distinct 'bizarre' mt tRNAsSer by alternative combination of interaction sites. © 2005 European Molecular Biology Organization | All Rights Reserved.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=27144454126&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/16286
ISSN: 14602075
02614189
Appears in Collections:Scopus 2001-2005

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