About: Site specific target binding controls RNA cleavage efficiency by the Kaposi’s sarcoma-associated herpesvirus endonuclease SOX

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About: Site specific target binding controls RNA cleavage efficiency by the Kaposi’s sarcoma-associated herpesvirus endonuclease SOX Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Site specific target binding controls RNA cleavage efficiency by the Kaposi’s sarcoma-associated herpesvirus endonuclease SOX
Creator	Bohne, Jens Vogt, Carolin Glaunsinger, Britt Mendez, Aaron
topic	covid:532dc582abd41e833303742ca40976db63fe6fc1#this
Source	BioRxiv; MedRxiv
abstract	During lytic replication of Kaposi’s sarcoma-associated herpesvirus (KSHV), the gene expression landscape of a cell is remodeled to evade the immune response and create an environment favorable to viral replication. A major driver of these gene expression changes is a virally encoded, messenger RNA (mRNA)-specific endonuclease termed SOX. SOX cleaves the majority of cytoplasmic mRNAs, but does so at specific internal sites loosely defined by a degenerate sequence motif. If and how RNA sequence directs SOX targeting remained unknown. To address these questions, we used recombinant, highly purified SOX endonuclease in a series of biochemical assays to reconstitute the cleavage reaction in vitro and gain significant insight into the biochemical mechanism of both SOX target recognition and endonucleolytic cleavage. Using this system, we determined that cut site specificity is preserved with purified SOX and a validated target RNA and thus does not require additional cellular cofactors. Furthermore, we showed that SOX displays robust, sequence-specific RNA binding to residues proximal to the cleavage site, which must be presented in a particular structural context. The strength of SOX binding dictates cleavage efficiency, providing an explanation for the breadth of target RNA susceptibility observed in cells. Kaposi’s sarcoma-associated herpesvirus (KSHV) is an oncogenic human virus that causes Kaposi’s sarcoma, primary effusion lymphoma, and multicentric Castleman disease. During viral replication, KSHV expresses an enzyme called SOX that cuts and inactivates the majority of cellular messenger RNAs, preventing their translation into proteins. Some mRNAs are efficiently cleaved by SOX, while others are poorly cleaved, but the mechanistic basis underlying this selectivity has remained largely unknown. Here, we reveal that the efficiency of RNA cleavage is heavily impacted by RNA sequences proximal to the cleavage site, which serve as a SOX binding platform. This helps explain both the range of RNA cleavage efficiency observed in SOX-expressing cells as well as the sequence specificity underlying SOX targeting.
has issue date	2018-05-13(xsd:dateTime)
bibo:doi	10.1101/320929
has license	medrxiv
sha1sum (hex)	532dc582abd41e833303742ca40976db63fe6fc1
schema:url	https://doi.org/10.1101/320929
resource representing a document's title	Site specific target binding controls RNA cleavage efficiency by the Kaposi’s sarcoma-associated herpesvirus endonuclease SOX
schema:publication	bioRxiv
resource representing a document's body	covid:532dc582abd41e833303742ca40976db63fe6fc1#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/532dc582abd41e833303742ca40976db63fe6fc1
is schema:about of	named entity 'CLASSIFICATION' named entity 'BIOLOGY' named entity 'RNA CLEAVAGE' named entity 'cleavage' named entity 'SOX' named entity 'bioRxiv' named entity 'cleavage' named entity 'biochemical assays' named entity 'directs' named entity '27S' named entity 'TARGET' named entity 'CUT' named entity 'BIOCHEMICAL' named entity 'INSIGHT' named entity 'SITES' named entity 'RNA' named entity 'ENVIRONMENT' named entity 'SITE SPECIFIC' named entity 'OBSERVED' named entity 'STRUCTURAL' named entity 'FAVORABLE' named entity 'MESSENGER RNA' named entity 'DOES NOT' named entity 'EFFICIENCY' named entity 'BIOLOGICAL SCIENCES' named entity 'KAPOSI' named entity 'EFFICIENCY' named entity 'RECOGNITION' named entity 'CREATE' named entity 'INTERNAL' named entity 'VALIDATED' named entity 'DETERMINED' named entity 'SPECIFIC' named entity 'USING' named entity 'HIGHLY' named entity 'PRESENTED' named entity 'SOX' named entity 'COFACTORS' named entity 'DEFINED' named entity 'ENDONUCLEASE' named entity 'CLEAVAGE' named entity 'BREADTH' named entity 'SOX' named entity 'MINOR' named entity 'PROXIMAL TO' named entity 'EXPLANATION' named entity 'KAPOSI' named entity 'DOI' named entity 'RECOMBINANT' named entity 'CYTOPLASMIC' named entity 'CELLS' named entity 'DISPLAYS' named entity 'LYTIC' named entity 'ASSOCIATED' named entity 'BINDING' named entity 'SARCOMA' named entity 'HERPESVIRUS' named entity 'MICROBIAL' named entity 'ADDITIONAL' named entity 'RECONSTITUTE' named entity 'BIOCHEMICAL MECHANISM' named entity 'PRESERVED' named entity 'PREPRINT' named entity 'SYSTEM' named entity 'SIGNIFICANT' named entity 'SITE SPECIFICITY' named entity 'VIRAL REPLICATION' named entity '2F10' named entity 'BUT' named entity 'AUTHOR' named entity 'RNA SEQUENCE' named entity 'PEER-REVIEWED' named entity 'STRENGTH' named entity 'TARGETING' named entity 'TARGET' named entity 'CELLULAR' named entity 'SEQUENCE MOTIF' named entity 'PURIFIED' named entity 'SEQUENCE'

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