dc.creatorManzine, Livia Regina
dc.creatorSerrão, Vitor Hugo Balasco
dc.creatorLima, Luis Maurício Trambaioli da Rocha e
dc.creatorSouza, Marcos Michel de
dc.creatorBettini, Jefferson
dc.creatorPortugal, Rodrigo Villares
dc.creatorHeel, Marin van
dc.creatorThiemann, Otavio Henrique
dc.date.accessioned2014-05-23T17:43:46Z
dc.date.accessioned2018-07-04T16:45:58Z
dc.date.available2014-05-23T17:43:46Z
dc.date.available2018-07-04T16:45:58Z
dc.date.created2014-05-23T17:43:46Z
dc.date.issued2013-04
dc.identifierFEBS Letters, Amsterdam : Elsevier BV, v. 587, n. 7, p. 906-911, Apr. 2013
dc.identifier0014-5793
dc.identifierhttp://www.producao.usp.br/handle/BDPI/45006
dc.identifier10.1016/j.febslet.2013.02.014
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1640071
dc.description.abstractIn bacteria selenocysteyl-tRNAsec (SelC) is synthesized by selenocysteine synthase (SelA). Here we show by fluorescence anisotropy binding assays and electron microscopical symmetry analysis that the SelA-tRNAsec binding stoichiometry is of one tRNAsec molecule per SelA monomer (1:1) rather than the 1:2 value proposed previously. Negative stain transmission electron microscopy revealed a D5 pointgroup symmetry for the SelA-tRNAsec assembly both with and without tRNAsec bound. Furthermore, SelA can associate forming a supramolecular complex of stacked decamer rings, which does not occur in the presence of tRNAsec. We discuss the structure-function relationships of these assemblies and their regulatory role in bacterial selenocysteyl-tRNAsec synthesis.
dc.languageeng
dc.publisherElsevier BV
dc.publisherAmsterdam
dc.relationFEBS Letters
dc.rightsCopyright Elsevier B.V.
dc.rightsrestrictedAccess
dc.subjectSelenocysteine synthase
dc.subjecttRNAsec
dc.subjectStoichiometry
dc.titleAssembly stoichiometry of bacterial selenocysteine synthase and SelC (tRNAsec)
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución