About: Identification and functional characterization of regions that can be crosslinked to RNA in the helicase-like domain of BaMV replicase

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About: Identification and functional characterization of regions that can be crosslinked to RNA in the helicase-like domain of BaMV replicase Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Identification and functional characterization of regions that can be crosslinked to RNA in the helicase-like domain of BaMV replicase
Creator	Hsu, Yau-Heiu Meng, Menghsiao Han, Yu-Tsung Lo, Chia-Wen
Source	Elsevier; Medline; PMC
abstract	Abstract The helicase-like domain of the Bamboo mosaic virus replicase catalyzes the release of 5′-γ-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 ∼20% replication efficiency was retained in protoplasts. R597A and K610A retained ∼50 and ∼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.
has issue date	2009-07-05(xsd:dateTime)
bibo:doi	10.1016/j.virol.2009.04.013
bibo:pmid	19443005
has license	els-covid
sha1sum (hex)	b8f9525f63118ab787c2f81dc9fff88cba0eecc7
schema:url	https://doi.org/10.1016/j.virol.2009.04.013
resource representing a document's title	Identification and functional characterization of regions that can be crosslinked to RNA in the helicase-like domain of BaMV replicase
has PubMed Central identifier	PMC7134557
has PubMed identifier	19443005
schema:publication	Virology
resource representing a document's body	covid:b8f9525f63118ab787c2f81dc9fff88cba0eecc7#body_text
is schema:about of	named entity 'IDENTIFICATION' named entity 'mutations' named entity 'plants' named entity 'domain' named entity 'RNA' named entity 'LIMITED BY' named entity '20%' named entity 'REGIONS' named entity 'GREATLY' named entity 'MUTATIONAL ANALYSIS' named entity 'EXTREMELY LIMITED' named entity 'RNA BINDING' named entity 'RETAINED' named entity 'VIRAL REPLICATION' named entity 'RNA' named entity 'CELL MOVEMENT' named entity 'MAPPED' named entity 'RELEASE' named entity 'SYSTEMIC' named entity 'FUNCTIONAL' named entity 'DOMAIN' named entity 'BINDING' named entity 'PHOSPHATE' named entity 'CELL' named entity 'DIMINISHED' covid:arg/b8f9525f63118ab787c2f81dc9fff88cba0eecc7 named entity 'CROSSLINKED' named entity 'ENZYMATIC' named entity 'ATP' named entity 'HELICASE' named entity 'PROTEINS' named entity 'INVOLVED' named entity 'REGIONS' named entity 'RNA' named entity 'DECREASED ACTIVITY' named entity 'CROSSLINKING' named entity 'BAMBOO MOSAIC VIRUS' named entity 'MOVEMENT' named entity 'SET' named entity 'ACTIVITIES' named entity 'VIRAL' named entity 'RESTRICTED' named entity 'DIFFERENT' named entity 'MUTANTS' named entity 'STUDY' named entity 'PRESENT' named entity 'NICOTIANA BENTHAMIANA' named entity 'PEPTIDYL' named entity 'LEVELS' named entity 'REVERSIBLE' named entity 'EXAMINED' named entity 'REPLICASE' named entity 'FORMALDEHYDE' named entity 'LIKE' named entity 'PROTOPLASTS' named entity 'MASS SPECTROMETRY' named entity 'MUTATIONS' named entity 'REPLICATION' named entity '80%' named entity 'EFFICIENCY' named entity 'CATALYTIC' named entity 'DOMAIN' named entity 'LARGER' named entity 'PLANTS' named entity 'CHARACTERIZATION' named entity 'HELICASE' named entity 'IDENTICAL' named entity 'REPLICASE' named entity 'SUBSTRATE' named entity 'LIKE' named entity '90%' named entity 'THESE' named entity 'TO SUPPORT' named entity 'replicase' named entity 'catalyzes' named entity 'mutants' named entity 'substrate' named entity 'protoplasts'

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