Regulation of maize lysine metabolism and endosperm protein synthesis by opaque and floury mutations

dc.creatorAzevedo, RA
dc.creatorDamerval, C
dc.creatorLandry, J
dc.creatorLea, PJ
dc.creatorBellato, CM
dc.creatorMeinhardt, LW
dc.creatorLe Guilloux, M
dc.creatorDelhaye, S
dc.creatorToro, AA
dc.creatorGaziola, SA
dc.creatorBerdejo, BDA
dc.date2003
dc.dateDEC
dc.date2014-11-15T12:13:27Z
dc.date2015-11-26T17:19:53Z
dc.date2014-11-15T12:13:27Z
dc.date2015-11-26T17:19:53Z
dc.date.accessioned2018-03-29T00:07:32Z
dc.date.available2018-03-29T00:07:32Z
dc.identifierEuropean Journal Of Biochemistry. Wiley-blackwell, v. 270, n. 24, n. 4898, n. 4908, 2003.
dc.identifier0014-2956
dc.identifierWOS:000187006500011
dc.identifier10.1046/j.1432-1033.2003.03890.x
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/80063
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/80063
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/80063
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1283007
dc.descriptionThe capacity of two maize opaque endosperm mutants (o1 and o2) and two floury (fl1 and fl2) to accumulate lysine in the seed in relation to their wild type counterparts Oh43+ was examined. The highest total lysine content was 3.78% in the o2 mutant and the lowest 1.87% in fl1, as compared with the wild type (1.49%). For soluble lysine, o2 exhibited over a 700% increase, whilst for fl3 a 28% decrease was encountered, as compared with the wild type. In order to understand the mechanisms causing these large variations in both total and soluble lysine content, a quantitative and qualitative study of the N constituents of the endosperm has been carried out and data obtained for the total protein, nonprotein N, soluble amino acids, albumins/globulins, zeins and glutelins present in the seed of the mutants. Following two-dimensional PAGE separation, a total of 35 different forms of zein polypeptides were detected and considerable differences were noted between the five different lines. In addition, two enzymes of the aspartate biosynthetic pathway, aspartate kinase and homoserine dehydrogenase were analyzed with respect to feedback inhibition by lysine and threonine. The activities of the enzymes lysine 2-oxoglutate reductase and saccharopine dehydrogenase, both involved in lysine degradation in the maize endosperm were also determined and shown to be reduced several fold with the introduction of the o2, fl1 and fl2 mutations in the Oh43+ inbred line, whereas wild-type activity levels were verified in the Oh43o1 mutant.
dc.description270
dc.description24
dc.description4898
dc.description4908
dc.languageen
dc.publisherWiley-blackwell
dc.publisherHoboken
dc.publisherEUA
dc.relationEuropean Journal Of Biochemistry
dc.relationEur. J. Biochem.
dc.rightsfechado
dc.rightshttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.sourceWeb of Science
dc.subjectlysine metabolism
dc.subjectmaize
dc.subjectstorage proteins
dc.subjectReductase-saccharopine Dehydrogenase
dc.subjectInsensitive Aspartate Kinase
dc.subjectAmino-acid Content
dc.subjectBifunctional Enzyme
dc.subjectTranscriptional Activator
dc.subjectHigher-plants
dc.subjectKetoglutarate Reductase
dc.subjectPhaseolus-vulgaris
dc.subjectRice Seeds
dc.subjectGene
dc.titleRegulation of maize lysine metabolism and endosperm protein synthesis by opaque and floury mutations
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución