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Titolo:
CLONING OF THE GENE FOR MONOGALACTOSYLDIACYLGLYCEROL SYNTHASE AND ITSEVOLUTIONARY ORIGIN
Autore:
SHIMOJIMA M; OHTA H; IWAMATSU A; MASUDA T; SHIOI Y; TAKAMIYA K;
Indirizzi:
TOKYO INST TECHNOL,FAC BIOSCI & BIOTECHNOL,DEPT BIOL SCI,MIDORI KU,4259 NAGATSUTA YOKOHAMA KANAGAWA 226 JAPAN TOKYO INST TECHNOL,FAC BIOSCI & BIOTECHNOL,DEPT BIOL SCI,MIDORI KU YOKOHAMA KANAGAWA 226 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL,KANAZAWA KU YOKOHAMA KANAGAWA 236 JAPAN SHIZUOKA UNIV,DEPT BIOL & GEOSCI,FAC SCI SHIZUOKA 422 JAPAN
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 1, volume: 94, anno: 1997,
pagine: 333 - 337
SICI:
0027-8424(1997)94:1<333:COTGFM>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHLOROPLAST ENVELOPE MEMBRANES; ESCHERICHIA-COLI; UDP-GALACTOSE; DIACYLGLYCEROL GALACTOSYLTRANSFERASE; PHOTOSYNTHETIC MEMBRANES; NUCLEOTIDE-SEQUENCE; CELL-DIVISION; MURG GENE; PEPTIDOGLYCAN; GALACTOLIPIDS;
Keywords:
GALACTOSYLTRANSFERASE; ENDOSYMBIOSIS; CHLOROPLAST MEMBRANE; PEPTIDOGLYCAN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
M. Shimojima et al., "CLONING OF THE GENE FOR MONOGALACTOSYLDIACYLGLYCEROL SYNTHASE AND ITSEVOLUTIONARY ORIGIN", Proceedings of the National Academy of Sciences of the United Statesof America, 94(1), 1997, pp. 333-337

Abstract

Monogalactosyldiacylglycerol (MGDG) synthase (UDPgalactose:1,2-diacylglycerol 3-beta-D-galactosyltransferase; EC 2.4.1.46) catalyzes formation of MGDG, a major structural lipid of chloroplast. We cloned a cDNAfor the synthase from cucumber cDNA library. The full-length cDNA clone was 2142 bp, and it contains a 1575-bp open reading frame encoding 525 aa. The open reading frame consists of the regions for a mature protein (422 aa; M(r) of 46,552) and transit peptide to chloroplast (103aa). Although the molecular weight of mature protein region matched that purified from cucumber cotyledons, it was quite different from those purified from spinach (approximate to 20 kDa) reported by other groups. The mature region of the protein was expressed in Escherichia coli as a fusion protein with glutathione S-transferase. The expression in E. coli showed that the protein catalyzed MGDG synthesis very efficiently. Therefore, we concluded that the cDNA encodes MGDG synthase in cucumber. In addition, the deduced amino acid sequence of the MGDG synthase cDNA showed homology with MurG of Bacillus subtilis and E. coli,which encode a glycosyltransferase catalyzing the last step of peptidoglycan synthesis in bacteria. This sequence homology implies that themachinery of chloroplast membrane biosynthesis is evolutionarily derived from that of cell wall biosynthesis in bacteria. This is consistent with the endosymbiotic hypothesis of chloroplast formation.

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Documento generato il 20/01/21 alle ore 03:06:39