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|標題:||Identification and functional characterization of regions that can be crosslinked to RNA in the helicase-like domain of BaMV replicase||作者:||Han, Y.T.
|關鍵字:||RNA-binding;5 '-Triphosphatase;Helicase;Bamboo mosaic virus;Reversible formaldehyde crosslinking;bamboo mosaic potexvirus;hepatitis-c virus;5'-triphosphatase activity;rig-i;antiviral responses;protein;dna;1a;polymerase;complexes||Project:||Virology||期刊/報告no：:||Virology, Volume 389, Issue 1-2, Page(s) 34-44.||摘要:||
The helicase-like domain of the Bamboo mosaic virus replicase catalyzes the release of 5'-gamma-phosphate from both ATP and 5'-triphosphated RNA by an identical set of catalytic residues with a presumably larger binding pocket for RNA. In this study, the peptidyl regions involved in RNA binding were mapped by reversible formaldehyde crosslinking and mass spectrometry. Eleven residues within these regions were examined by mutational analysis. H636A, Y704A, and K706A greatly diminished the enzymatic activities and were unable to support the viral replication in Nicotiana benthamiana protoplasts. K843A decreased activity toward the RNA substrate to 17% of WT and similar to 20% replication efficiency was retained in protoplasts. R597A and K610A retained similar to 50 and similar to 90% of the enzymatic activities, respectively. However, replication in protoplasts of these mutants was extremely limited. Proteins with the mutations K603A, R628A, R645A, H794A, and R799A were present at levels 30-69% of WT in protoplasts. However, the fates of these mutations in plants were different. Viral cell-to-cell movement was limited by the K603A and R628A mutations, while systemic movement was restricted by R645A and H794A. The implications of the helicase-like domain in the viral replication and movement are discussed. (c) 2009 Elsevier Inc. All rights reserved.
|Appears in Collections:||生物科技學研究所|
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