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https://doi.org/10.1371/journal.ppat.1001038
Title: | The N-terminal domain of the arenavirus L protein is an RNA endonuclease essential in mRNA transcription | Authors: | Morin B. Coutard B. Lelke M. Ferron F. Kerber R. Jamal S. Frangeul A. Baronti C. Charrel R. de Lamballerie X. Vonrhein C. Lescar J. Bricogne G. Günther S. Canard B. |
Keywords: | arenavirus L protein messenger RNA unclassified drug virus protein amino terminal sequence Arenavirus article controlled study crystal structure enzyme active site enzyme activity Lymphocytic choriomeningitis virus mutagenesis mutational analysis nonhuman protein cross linking replicon RNA binding RNA replication RNA transcription virus characterization Bunyaviridae Catalytic Domain Crystallization Crystallography, X-Ray Endonucleases Endoribonucleases Lymphocytic choriomeningitis virus Models, Molecular Mutagenesis Orthomyxoviridae Protein Structure, Tertiary RNA, Messenger RNA, Viral Transcription, Genetic Arenaviridae Arenavirus Bunyaviridae Lymphocytic choriomeningitis virus Orthomyxoviridae |
Issue Date: | 2010 | Publisher: | Public Library of Science | Citation: | Morin B., Coutard B., Lelke M., Ferron F., Kerber R., Jamal S., Frangeul A., Baronti C., Charrel R., de Lamballerie X., Vonrhein C., Lescar J., Bricogne G., Günther S., Canard B. (2010). The N-terminal domain of the arenavirus L protein is an RNA endonuclease essential in mRNA transcription. PLoS Pathogens 6 (9) : e01038. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.ppat.1001038 | Abstract: | Arenaviridae synthesize viral mRNAs using short capped primers presumably acquired from cellular transcripts by a 'cap- snatching' mechanism. Here, we report the crystal structure and functional characterization of the N-terminal 196 residues (NL1) of the L protein from the prototypic arenavirus: lymphocytic choriomeningitis virus. The NL1 domain is able to bind and cleave RNA. The 2.13 A° resolution crystal structure of NL1 reveals a type II endonuclease α/β architecture similar to the N-terminal end of the influenza virus PA protein. Superimposition of both structures, mutagenesis and reverse genetics studies reveal a unique spatial arrangement of key active site residues related to the PD...(D/E)XK type II endonuclease signature sequence. We show that this endonuclease domain is conserved and active across the virus families Arenaviridae, Bunyaviridae and Orthomyxoviridae and propose that the arenavirus NL1 domain is the Arenaviridae cap-snatching endonuclease. © 2010 Morin et al. | Source Title: | PLoS Pathogens | URI: | https://scholarbank.nus.edu.sg/handle/10635/165417 | ISSN: | 15537366 | DOI: | 10.1371/journal.ppat.1001038 |
Appears in Collections: | Staff Publications Elements |
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