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dc.creatorSousa Martín, Carolinaes
dc.creatorKotrba, Paveles
dc.creatorRuml, Tomášes
dc.creatorCebolla, Ángeles
dc.creatorLorenzo, Víctor dees
dc.date.accessioned2016-06-07T10:49:45Z
dc.date.available2016-06-07T10:49:45Z
dc.date.issued1998
dc.identifier.citationSousa Martín, C., Kotrba, P., Ruml, T., Cebolla, Á. y Lorenzo, V.d. (1998). Metalloadsorption by Escherichia coli cells displaying yeast and mammalian metallothioneins anchored to the outer membrane protein LamB. Journal of Bacteriology, 180 (9), 2280-2284.
dc.identifier.issn0021-9193es
dc.identifier.urihttp://hdl.handle.net/11441/41987
dc.description.abstractYeast (CUP1) and mammalian (HMT-1A) metallothioneins (MTs) have been efficiently expressed in Escherichia coli as fusions to the outer membrane protein LamB. A 65-amino-acid sequence from the CUP1 protein of Saccharomyces cerevisiae (yeast [Y] MT) was genetically inserted in permissive site 153 of the LamB sequence, which faces the outer medium. A second LamB fusion at position 153 was created with 66 amino acids recruited from the form of human (H) MT that is predominant in the adipose tissue, HMT-1A. Both LamB153- YMT and LamB153-HMT hybrids were produced in vivo as full-length proteins, without any indication of instability or proteolytic degradation. Each of the two fusion proteins was functional as the port of entry of lambda phage variants, suggesting maintenance of the overall topology of the wild-type LamB. Expression of the hybrid proteins in vivo multiplied the natural ability of E. coli cells to bind Cd21 15- to 20-fold, in good correlation with the number of metal-binding centers contributed by the MT moiety of the fusionses
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherAmerican Society for Microbiologyes
dc.relation.ispartofJournal of Bacteriology, 180 (9), 2280-2284.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleMetalloadsorption by Escherichia coli cells displaying yeast and mammalian metallothioneins anchored to the outer membrane protein LamBes
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Microbiología y Parasitologíaes
dc.relation.publisherversionhttp://0-jb.asm.org.fama.us.es/content/180/9/2280.full.pdf+htmles
idus.format.extent5 p.es
dc.journaltitleJournal of Bacteriologyes
dc.publication.volumen180es
dc.publication.issue9es
dc.publication.initialPage2280es
dc.publication.endPage2284es
dc.identifier.idushttps://idus.us.es/xmlui/handle/11441/41987

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