About: The SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-Quadruplexes

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About: The SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-Quadruplexes Goto Sponge NotDistinct Permalink

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Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	The SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-Quadruplexes
Creator	Hilgenfeld, Rolf Vonrhein, Clemens Kusov, Yuri Tan, Jinzhi Bollati, Michela Bricogne, Gerard Hansen, Guido Mesters, Jeroen Schmidt, Christian Smart, Oliver
source	Medline; PMC
abstract	Since the outbreak of severe acute respiratory syndrome (SARS) in 2003, the three-dimensional structures of several of the replicase/transcriptase components of SARS coronavirus (SARS-CoV), the non-structural proteins (Nsps), have been determined. However, within the large Nsp3 (1922 amino-acid residues), the structure and function of the so-called SARS-unique domain (SUD) have remained elusive. SUD occurs only in SARS-CoV and the highly related viruses found in certain bats, but is absent from all other coronaviruses. Therefore, it has been speculated that it may be involved in the extreme pathogenicity of SARS-CoV, compared to other coronaviruses, most of which cause only mild infections in humans. In order to help elucidate the function of the SUD, we have determined crystal structures of fragment 389–652 (“SUD(core)”) of Nsp3, which comprises 264 of the 338 residues of the domain. Both the monoclinic and triclinic crystal forms (2.2 and 2.8 Å resolution, respectively) revealed that SUD(core) forms a homodimer. Each monomer consists of two subdomains, SUD-N and SUD-M, with a macrodomain fold similar to the SARS-CoV X-domain. However, in contrast to the latter, SUD fails to bind ADP-ribose, as determined by zone-interference gel electrophoresis. Instead, the entire SUD(core) as well as its individual subdomains interact with oligonucleotides known to form G-quadruplexes. This includes oligodeoxy- as well as oligoribonucleotides. Mutations of selected lysine residues on the surface of the SUD-N subdomain lead to reduction of G-quadruplex binding, whereas mutations in the SUD-M subdomain abolish it. As there is no evidence for Nsp3 entering the nucleus of the host cell, the SARS-CoV genomic RNA or host-cell mRNA containing long G-stretches may be targets of SUD. The SARS-CoV genome is devoid of G-stretches longer than 5–6 nucleotides, but more extended G-stretches are found in the 3′-nontranslated regions of mRNAs coding for certain host-cell proteins involved in apoptosis or signal transduction, and have been shown to bind to SUD in vitro. Therefore, SUD may be involved in controlling the host cell's response to the viral infection. Possible interference with poly(ADP-ribose) polymerase-like domains is also discussed.
has issue date	2009-05-15(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1000428
bibo:pmid	19436709
has license	cc-by
sha1sum (hex)	3f962f74bcf72c06a4f0941b8da40742024dae3f
schema:url	https://doi.org/10.1371/journal.ppat.1000428
resource representing a document's title	The SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-Quadruplexes
has PubMed Central identifier	PMC2674928
has PubMed identifier	19436709
schema:publication	PLoS Pathog
resource representing a document's body	covid:3f962f74bcf72c06a4f0941b8da40742024dae3f#body_text
is schema:about of	named entity 'SARS-CoV' named entity 'determined' named entity 'Domain' named entity 'G-QUADRUPLEXES' named entity 'HOST CELL' named entity 'INTERFERENCE' named entity 'MUTATIONS' named entity 'STRETCHES' named entity 'CRYSTAL' named entity 'LIKE' named entity 'ORDER' named entity 'RESOLUTION' named entity 'RESPONSE TO' named entity 'ITS' named entity 'INVOLVED' named entity 'TARGETS' named entity 'UNIQUE' named entity 'SUBDOMAIN' named entity 'KNOWN' named entity 'NUCLEOTIDES' named entity 'EXTREME' named entity 'REPLICASE' named entity 'TRICLINIC' named entity 'APOPTOSIS' named entity 'CORE' named entity 'CONTROLLING' named entity 'BIND' named entity 'COMPARED' named entity 'POSSIBLE' named entity 'SUD' named entity 'ZONE' named entity 'POLYMERASE' named entity 'RELATED' named entity 'ENTIRE' named entity 'LEAD' named entity 'CELL' named entity 'FUNCTION' named entity 'OUTBREAK' named entity 'FOLD' named entity 'VIRUSES' named entity '652' named entity 'MONOMER' named entity 'NUCLEUS' named entity 'TO HELP' named entity 'REGIONS' named entity 'OLIGONUCLEOTIDES' named entity 'OLIGORIBONUCLEOTIDES' named entity 'HOMODIMER' named entity 'ABSENT' named entity 'SIMILAR' named entity 'NON-STRUCTURAL PROTEINS' named entity '27S' named entity 'FRAGMENT' named entity 'FORMS' named entity 'MILD' named entity 'RIBOSE' named entity 'BIND' named entity 'DOMAIN' named entity 'GEL ELECTROPHORESIS' named entity 'BINDING' named entity '389' named entity 'RNA' named entity 'PATHOGENICITY' named entity 'CAUSE' named entity 'TO BIND TO' named entity 'LONG' named entity 'DOMAIN' named entity 'REVEALED' named entity 'SIGNAL TRANSDUCTION' named entity 'CODING' named entity 'HIGHLY' named entity 'G-QUADRUPLEXES'

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