Restoration of potato virus X coat protein capacity for assembly with RNA after His-tag removal View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-02

AUTHORS

Olga Zayakina, Marina Arkhipenko, Alexander Smirnov, Nina Rodionova, Olga Karpova, Joseph Atabekov

ABSTRACT

We found that the fusion of hexahistidine (H)6 tag to the potato virus X (PVX) coat protein (CP) abolished its ability to be assembled with viral RNA into helical nucleoprotein virus-like particles (VLPs). Instead, irregular agglomerates were produced upon incubation of PVX RNA with (H)6-tagged PVX CP. A factor Xa recognition site, IEGR, was inserted upstream of the CP coding sequence. Removal of the (H)6 tag from PVX CP by Xa protease restored its ability to bind RNA and to assemble VLPs. In addition to the canonical IEGR site, the factor Xa protease was found to cleave PVX CP at a second (non-consensus) site, AVTRGR, located close to the C-terminus of PVX CP. The latter cleavage did not affect reassembly of the PVX RNA and CP into VLPs. More... »

PAGES

337-341

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00705-008-0299-z

DOI

http://dx.doi.org/10.1007/s00705-008-0299-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029717581

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19130167


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