Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/4645
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dc.contributor.authorDechamma, H J-
dc.contributor.authorkumar, C Ashok-
dc.contributor.authorNagarajan, G-
dc.contributor.authorSuryanarayana, V V S-
dc.date.accessioned2009-06-16T03:34:31Z-
dc.date.available2009-06-16T03:34:31Z-
dc.date.issued2008-11-
dc.identifier.issn0975-1009 (Online); 0019-5189 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/4645-
dc.description760-763en_US
dc.description.abstractExpressions of several genes in bacteria were carried out by independent promoter. However, in case of eukaryotes ribosome skipping and introduction of IRES are employed as alternative to multiple translation initiation. Foot and mouth disease virus (FMDV) 2A peptide has been widely used for co-expression of multiple genes in eukaryotic, plant and mammalian systems. The 18 amino acid 2A peptide of FMDV facilitates efficient co-translational dissociation of the polyprotein into discrete protein products. To study the role of 2A in multimeric protein production a construct consisting of tandem repeat of 4 units of C- terminal VP1 linked through 2A sequence was made and expressed in E. coli. Along with tetramer protein, trimer, dimer and monomer proteins were produced. Stability studies showed that the tetramer protein was cleaved to smaller monomer on storage. The results provide scope for using FMDV 2A for expressing multiple genes under a single promoter in prokaryotes.en_US
dc.language.isoen_USen_US
dc.publisherCSIRen_US
dc.sourceIJEB Vol.46(11) [November 2008]en_US
dc.subjectExpressionen_US
dc.subjectFoot and mouth diseaseen_US
dc.subjectMultigeneen_US
dc.subject2A Peptideen_US
dc.subjectProteolysisen_US
dc.titleProcessing of multimer FMD virus VP1-2A protein expressed in E. coli into monomersen_US
dc.typeArticleen_US
Appears in Collections:IJEB Vol.46(11) [November 2008]

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