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Titolo:
Molecular consequences of Ds insertion into and excision from the helix-loop-helix domain of the maize R gene
Autore:
Liu, YH; Wang, LJ; Kermicle, JL; Wessler, SR;
Indirizzi:
Univ Georgia, Dept Genet, Athens, GA 30602 USA Univ Georgia Athens GA USA30602 eorgia, Dept Genet, Athens, GA 30602 USA Univ Georgia, Dept Bot, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Georgia, Dept Bot, Athens, GA 30602 USA Univ Wisconsin, Genet Lab, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 sin, Genet Lab, Madison, WI 53706 USA
Titolo Testata:
GENETICS
fascicolo: 4, volume: 150, anno: 1998,
pagine: 1639 - 1648
SICI:
0016-6731(199812)150:4<1639:MCODII>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSPOSABLE ELEMENT DISSOCIATION; CHALCONE SYNTHASE GENES; REGULATORY GENES; ZEA-MAYS; ANTHOCYANIN PRODUCTION; NUCLEOTIDE-SEQUENCE; TRANSCRIPTIONAL ACTIVATORS; NUCLEAR-LOCALIZATION; PROTEIN; LOCUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Wessler, SR Univ Georgia, Dept Genet, Life Sci Bldg, Athens, GA 30602 USA Univ Georgia Life Sci Bldg Athens GA USA 30602 s, GA 30602 USA
Citazione:
Y.H. Liu et al., "Molecular consequences of Ds insertion into and excision from the helix-loop-helix domain of the maize R gene", GENETICS, 150(4), 1998, pp. 1639-1648

Abstract

The R and B proteins of maize are required to activate the transcription of several genes in the anthocyanin biosynthetic pathway. To determine the structural requirements for R function in vivo, we are exploiting its sensitive mutant phenotype to identify transposon (Ds) insertions that disrupt critical domains. Here we report that the ability of the r-m1 allele to activate transcription of at least three structural genes is reduced to only 2% of wild-type activity because of a 396-bp Ds element in helix 2 of the basic helix-loop-helix (bHLH) motif. Residual activity likely results from the synthesis of a mutant protein that contains seven additional amino acids inhelix 2. This protein is encoded by a transcript where most of the Ds sequence has been spliced from pre-mRNA. Two phenotypic classes of stable derivative alleles, very pale and extremely pale, condition <1% of wild-type activity as a result of the presence of two- and three-amino-acid insertions, respectively, at the site of Ds excision. Localization of these mutant proteins to the nucleus indicates a requirement for an intact bHLH domain afternuclear import. The fact that deletion of the entire bHLH domain has only a minor effect on R protein activity while these small insertions virtuallyabolish activity suggests that deletion of the bHLH domain may bypass a requirement for bHLH-mediated protein-protein interactions in the activation of the structural genes in the anthocyanin biosynthetic pathway.

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Documento generato il 23/01/21 alle ore 10:10:06