Structure of the spinach chloroplast genes for the D2 and 44 kd reaction-centre proteins of pbotosystem II and for tRNA^Ser(UGA)

Abstract

We have determined the sequence of the spinach (Spinacia oleracea) chloroplast genes for the photosystem II proteins, D2 and the 44 kd reaction-centre, chlorophyll a-binding protein, and for tRNASer (UGA). The 3' end of the D2 gene overlaps the first 50 bp of the 5' end of the gene for the 44 kd protein. Northern RNA hybridization analysis indicates the two genes are cotranscribed into a single 3.5 kb RNA. The predicted molecular weight of the 353-residue D2 protein is 39536 and that of the 473-residue 44 kd protein is 51816. Both proteins are hydrophobic containing at least five possible membrane-spanning domains. D2 shows significant homology to the 32 kd herbicide-binding protein (Zurawski et al., (1982) Proc. Natl. Acad. Sci. USA 79, 7699-7703), and parts of the 44 kd protein show obvious similarities to parts of the 51 kd reaction-centre, chlorophyll a-binding protein of photosystem II (Morris and Herrmann (1984) Nucleic Acids Res. 12, 2837-2850). The gene for tRNASer (UGA) which is on the opposite strand to and transcribed towards the photosystem II genes is 72% homologous with the corresponding Escherichia coli tRNASer.

Isolation of the photosystem II reaction center complex from barley. Characterization by circular dichroism spectroscopy and amino acid sequencing

“…Moreover the size of the isolated peptides was in agreement with the positions of glutamic and aspartic acid residues predicted from the gene sequence. That the barley sequence is so similar to the deduced spinach sequence and that an antibody raised against Chlamydomonas will precipitate an in vitro translated spinach protein supports our proposal in the introduction that Chl~-protein 2 is conserved to the same extent as the D2 and the 32 kD herbicide-binding polypepfide (3,13,15,22,37,50). In this connection it should be mentioned that the isolated peptides were derived from a relatively hydrophilic part of the molecule as judged from the deduced spinach protein sequence.…”

“…The nucleotide sequence of this gene has been determined in a variety of organisms, showing very few differences between cyanobacteria (13), Chlamydomonas (15) and higher plants (50). The sequence of the D2 membrane polypeptide from PSII is also conserved (3,22,37). The few differences occurring in the sequences of these polypeptides suggest that their tertiary structure and the architecture of the PSII core complex with which they interact may be equally conserved.…”

The Chloroplast trnT–trnF Region in the Seed Plant Lineage Gnetales

“…By forming hairpin structures, they may also function as transcription termination signals as has been found in operons originating from bacteria, including chloroplast operons (Bogorad 1991). Hairpin structures/inverted repeated sequences have been reported from the downstream of maize tRNA His (GUG) (Schwarz et al 1981) and tRNA Phe (UGU) (Steinmetz et al 1983), spinach tRNA Ser (UGA) (Holschuh et al 1984), tobacco tRNA Glu (UUC)-tRNA Tyr (GUA)-tRNA Asp (GUC) (Ohme et al 1985), and the Brassica napus rRNAs-tRNA Arg (ACG) operon (Leal-Klevezas et al 2000).…”

Immunological evidence for the presence of the D1 and D2 proteins in PS II cores of higher plants

“…PS II core preparations were made from pea using Triton X-100 by following the method of Gounaris and Barber [20]. This PS II core preparation is essentially free of the 33 kDa lysine-rich protein characterised by Murata and Kuwabara [21].…”