The structure of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from spinach chloroplast DNA

Abstract

A cloned fragment of spinach chloroplast DNA carrying the gene for the large subunit of ribulose bisphosphate (RuBP) carboxylase has been analysed by electron microscopy of R-loops, by hybridization to Northern blots of chloroplast RNA, by S1 nuclease mapping and by DNA sequencing. The transcribed region of the gene is 1690 +/- 3 nucleotides long and co-linear with its mRNA. It comprises a 178-179 bp 5' untranslated sequence, a 1425 bp coding region and an 85-88 bp 3' untranslated region. The deduced sequence of the 475 amino acids of the spinach large subunit protein shows 10% divergence from that of the maize large subunit protein (1). The nucleotide sequence divergence between spinach and maize over the same coding region is 16% but in the transcribed flanking regions it is 35%. Features of the spinach chloroplast gene which resemble those of bacterial genes include a 5-base Shine-Dalgarno sequence complementary to a sequence near the 3' end of chloroplast and bacterial 16S rRNA, a promoter region partially homologous to a consensus sequence of bacterial promoters, and a transcription termination region capable of forming a typical stem and loop structure.

Phylogeny and biogeographic diversification of Maianthemum (Ruscaceae: Polygonatae)

“…For trnL-F regions, primers c, d, e, and f as in Taberlet et al (1991) were used with the internal primers d and e used only for degraded DNA. For rbcL, primers Z1 and 3' (Zurawski et al, 1981;Olmstead et al, 1993) were used. In taxa for which the primer 3' failed to produce any readable sequences, another primer Z1204R was used (Zurawski et al, 1981).…”

“…For rbcL, primers Z1 and 3' (Zurawski et al, 1981;Olmstead et al, 1993) were used. In taxa for which the primer 3' failed to produce any readable sequences, another primer Z1204R was used (Zurawski et al, 1981). The following pairs were employed for the markers:…”

Purification, Characterization and Thermostability of Ribulose 1,5-Bisphosphate Carboxylase-Oxygenase from Barley Leaves

“…On the basis of available crystallographic (Andersson et al, 1989; Knight at al., 1989;1990;Taylor and Andersson, 1997) and gene struc tures (McIntosh et al, 1980;Zurawski et al, 1981;Shinozaki and Sugiura, 1982;Zurawski et al, 1986) which revealed the 123 residues for the small su bunit and 475 amino acid residues for the large subunits we have calculated the amino acid com positions of other native rubisco enzymes and sys tematically compared them with barley rubisco (Table II). Major differences have been observed in the amino acid composition of barley rubisco, where the concentration of Cys, Ser, Thr, lieu, Leu, Arg and Trp residues are quite variable as compared to the other higher plants.…”

“…The importance of rubisco in photosynthesis and photorespiration makes it a major object for many structural and functional studies (for re view see, Schneider et al, 1992; Hartman and The crystal and the gene structures of many higher plant rubisco enzymes and its subunits have been well established with spinach (Spinacia oleracea L., Taylor and Andersson, 1997;Zurawski et al, 1981;Knight et al, 1989), to bacco (Nicotiana tabacum L., Shinozaki and Sugiura, 1982;Mazur and Chui, 1985;Chapman et al, 1987;Chapman et al, 1988), maize (Zea mays L., McIntosh et al, 1980;Zurawski et al, 1984), pea (Pisum sativum L., Zurawski et al, 1986) and the partial gene sequence of the large su bunit from barley (Hordeum vulgare L., Zuraw ski et al , 1984). Results of these studies revealed that in most of the photosynthetic organisms, including higher plants, rubisco is a hexadecamer (Mr. 560 kDa) consisting of eight large (LS) and eight small (SS) subunits in an L8S8 arrangement.…”

An intra‐dimeric crosslink of large subunits of spinach ribulose‐1,5‐bisphosphate carboxylase/oxygenase is formed by oxidation of cysteine 247

“…Since amino acid sequences of spinach Rbu(l,5)P2ase subunits contain 10 cysteines (9 in the L subunit and 1 in the S subunit, see Martin, 1979;Zurawski et al, 1981), we reexamined the thiol content of the spinach enzyme. The presence of three cysteines in the S subunit was revealed by titration of thiol groups in preparations of S subunits that were isolated according to Andrews and Lorimer (1985), and by analysis of carboxymethylated S subunit following the reaction of spinach Rbu(l,S)P2ase with iodo[14C]acetate.…”