Localization and nucleotide sequence of the gene for the membrane polypeptide D2 from pea chloroplast DNA

Abstract

The gene for the membrane polypeptide D2 has been mapped on the pea (Pisum sativum) chloroplast genome. The nucleotide sequence of the gene and its flanking regions is presented. The only large open reading frame in the sequence codes for a protein of MW 39.5 kD. A potential ribosome binding site is located 6 nucleotides upstream from the initiation codon and there are two sets of putative promotor sequences in the 5' flanking region. The polypeptide has a high content of hydrophobic amino acids, predominatly grouped in clusters of 20 or more residues. The 3' end of the D2 gene is overlapped by 50 nucleotides of a second open reading frame (UORF I) which is at least 369 nucleotides long. Based on current data we suggest the D2 polypeptide to be a constituent of photosystem II (PSII).

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.…”

Studies on the Photoactivation of the Water-Oxidizing Enzyme

“…We note the considerable amino acid sequence homology between D2 and the 32 kD QB protein (39,42) and the likelihood of their close proximity. Thus, both proteins may be susceptible to attack by a single protease.…”

Primary structure of barley genes encoding quinone and chlorophylla binding proteins of photosystem II

“…Figure 4 shows an alignment of this sequence from barley with the 5' leader sequences of psbD from spinach (1), tobacco (42), liverwort (47) and pea (38). Starting from about position -36 bp the nucleic acid sequences exhibit a striking similarity towards position -1.…”

“…All four polypeptides are coded for by the chloroplast DNA and they have been mapped and sequenced in several higher plants as well as in green algae and cyanobacteria. Information on the D-1 coding gene psbA is reviewed in (23), that for the D-2 coding gene psbD is presented in (1,18,38,42,47), while the structure of the psbB gene, coding for the 47 kD apoprotein, and the psbC gene, coding for the 44 kD apoprotein, is reported in (1, 18, 2 l, 30, 42, 47). Transcriptional features of the genes for these proteins are complex in that hybridization of plastid RNA to the neighbouring psbD and psbC genes revealed a heterogenous population of RNA transcripts (1,3,33).…”