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dc.contributor.authorOffei, S.K.
dc.contributor.authorCoffin, R.S.
dc.contributor.authorCoutts, Robert H.A.
dc.date.accessioned2014-03-05T09:28:57Z
dc.date.available2014-03-05T09:28:57Z
dc.date.issued1995-06
dc.identifier.citationOffei , S K , Coffin , R S & Coutts , R H A 1995 , ' The tobacco necrosis virus p7a protein is a nucleic acid-binding protein ' , Journal of General Virology , vol. 76 , no. 6 , pp. 1493-1496 . https://doi.org/10.1099/0022-1317-76-6-1493
dc.identifier.issn0022-1317
dc.identifier.otherPURE: 1955459
dc.identifier.otherPURE UUID: a80c3a2d-cbce-4e60-9470-437725e7c356
dc.identifier.otherScopus: 0029050774
dc.identifier.urihttp://hdl.handle.net/2299/13015
dc.description.abstractThe two centrally located open reading frames (ORFs) of necroviruses may, by analogy with the similarly located and related ORFs of carmoviruses, be expected to have a function in virus movement in plants. In the case of tobacco necrosis virus (TNV) strain D these proteins both have a molecular mass of approximately 7 kDa and are thus known as p7a and p7b. We over-expressed p7a in Escherichia coli, separated it from bacterial proteins and renatured it on gels, and showed that p7a was able to bind single-stranded RNA and single-stranded DNA, but was unable to bind double-stranded DNA. These protein-nucleic acid complexes were stable at moderately high salt concentrations. Protein p7b could not be expressed in a number of bacterial systems. We speculate that in TNV, unlike some other viruses which encode a single movement protein with separate functional domains for RNA binding and plasmodesmatal targeting, p7a and p7b may respectively provide these functions on separate proteins.en
dc.format.extent4
dc.language.isoeng
dc.relation.ispartofJournal of General Virology
dc.titleThe tobacco necrosis virus p7a protein is a nucleic acid-binding proteinen
dc.contributor.institutionGeography, Environment and Agriculture
dc.contributor.institutionAgriculture, Veterinary and Food Sciences
dc.contributor.institutionCrop and Environmental Protection
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionDepartment of Human and Environmental Sciences
dc.description.statusPeer reviewed
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=0029050774&partnerID=8YFLogxK
dc.relation.schoolSchool of Life and Medical Sciences
dcterms.dateAccepted1995-06
rioxxterms.versionofrecordhttps://doi.org/10.1099/0022-1317-76-6-1493
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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