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Titolo:
THE SACCHAROMYCES-CEREVISIAE RIB4 GENE CODES FOR 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE INVOLVED IN RIBOFLAVIN BIOSYNTHESIS - MOLECULAR CHARACTERIZATION OF THE GENE AND PURIFICATION OF THE ENCODED PROTEIN
Autore:
GARCIARAMIREZ JJ; SANTOS MA; REVUELTA JL;
Indirizzi:
UNIV SALAMANCA,DEPT MICROBIOL & GENET E-37007 SALAMANCA SPAIN UNIV SALAMANCA,DEPT MICROBIOL & GENET E-37007 SALAMANCA SPAIN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 40, volume: 270, anno: 1995,
pagine: 23801 - 23807
SICI:
0021-9258(1995)270:40<23801:TSRGCF>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION INITIATION SITES; BACILLUS-SUBTILIS; TATA ELEMENTS; 2 GENES; YEAST; SEQUENCE; TRANSFORMATION; MUTAGENESIS; EF-1-ALPHA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
J.J. Garciaramirez et al., "THE SACCHAROMYCES-CEREVISIAE RIB4 GENE CODES FOR 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE INVOLVED IN RIBOFLAVIN BIOSYNTHESIS - MOLECULAR CHARACTERIZATION OF THE GENE AND PURIFICATION OF THE ENCODED PROTEIN", The Journal of biological chemistry, 270(40), 1995, pp. 23801-23807

Abstract

6,7-Dimethyl-8-ribityllumazine, the immediate biosynthetic precursor of riboflavin, is synthesized by con densation of 5 amino 6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy-2-butanone 4 phosphate. The gene coding for 6,7-dimethyl-8-ribityllumazine synthase in Saccharomyces cerevisiae (RIB4) has been cloned by functional complementation of a mutant accumulating 5-amino-6-ribitylamino-2,4( 1H, 3H) -pyrimidinedione, which can grow on riboflavin- or diacetyl-but not on 3,4-dihydroxy-2-butanone-supplemented media, Gene disruption of the chromosomal copy of RIB4 led to riboflavin auxotrophy and loss of enzyme activity, Nucleotide sequencing revealed a 169-base pair open reading frame encoding a 18.6-kDa protein. Hybridization analysis indicated that RIB4 is a single copy gene located on the left arm of chromosome XV. Overexpression of the RIB4 coding sequence in yeast cells under the control of the strong TEF1 promoter allowed ready purification of 6,7-dimethyl-8-ribityllumazine synthase to apparent homogeneity by a simple procedure. Initial structural characterization of 6,7-dimethyl-8-ribityllumazine synthase by gel filtration chromatography and both nondenaturing pore limit and SDS-polyacrylamide gel electrophoresis showed thatthe enzyme forms a pentamer of identical 16.8-kDa subunits. The derived amino acid sequence of RIB4 shows extensive homology to the sequences of the beta subunits of riboflavin synthase from Bacillus subtilis and other prokaryotes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 07:05:46