Synthesis of Electron Transfer Components of the Photosynthetic Apparatus

Gray, John C.; Dunn, P. P. J.; Eccles, Christopher J.; Hird, Sean M.; Newman, Barbara; Willey, David L.

doi:10.1007/978-1-4615-7598-6_10

Cited by 4 publications

(2 citation statements)

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“…The presequences of lumenal polypeptides are thought to have two domains, an N-terminal chloroplast import domain which is cleaved off in the stroma, and a C-terminal thylakoid transfer domain which is cleaved by a thylakoid protease distinct from that in the stroma [ 15]. In contrast, the polypeptides of the reaction centre complex are all encoded by chloroplast genes [14] and are inserted directly into the thylakoid membrane.…”

Section: Introductionmentioning

confidence: 99%

Characterization of cDNA clones encoding the extrinsic 23 kDa polypeptide of the oxygen-evolving complex of photosystem II in pea

et al. 1989

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The 23 kDa polypeptide of the oxygen-evolving complex of photosystem II has been extracted from pea photosystem II particles by washing with 1 M NaCl and purified by anion-exchange chromatography. The N-terminal amino acid sequence has been determined and specific antisera have been raised in rabbits and used to screen a pea-leaf cDNA library in lambda gt11. Determination of the nucleotide sequence of two clones provided the nucleotide sequence for the full 23 kDa polypeptide. The deduced amino acid sequence showed it to code for a mature protein of 186 amino acid residues with an N-terminal presequence of 73 amino acid residues showing a high degree of conservation with previously reported 23 kDa sequences from spinach and Chlamydomonas. Southern blots of genomic DNA from pea probed with the labelled cDNA gave rise to only one band suggesting that the protein is encoded by a single gene. Northern blots of RNA extracted from various organs indicated a message of approximately 1.1 kb, in good agreement with the size of the cDNA, in all chlorophyll-containing tissues. Western blots of protein extracted from the same organs indicated that the 23 kDa polypeptide was present in all major organs of the plant except the roots.

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Section: Introductionmentioning

confidence: 99%

Characterization of cDNA clones encoding the extrinsic 23 kDa polypeptide of the oxygen-evolving complex of photosystem II in pea

et al. 1989

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“…Nucleotide sequencing has revealed the presence of small open reading frames in chloroplast DNA that appear to be cotranscribed with known photosystem II genes. These include an open reading frame of 38 amino acids cotranscribed with the psbB and psbH genes and two open reading frames of 38 and 40 codons cotranscribed with the psbE and psbF genes for cytochrome b-559 [13]. The fact that these open reading frames are co-transcribed with known photosystem II polypeptides has led to speculation that they may also encode components of photosystem II [5].…”

Section: Introductionmentioning

confidence: 99%

A photosystem II polypeptide is encoded by an open reading frame co-transcribed with genes for cytochrome b-559 in wheat chloroplast DNA

et al. 1989

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The N-terminal amino acid sequence of a 3.2 kDa photosystem II polypeptide is shown to be identical to that of a polypeptide encoded by an open reading frame of 38 codons (orf38) in wheat chloroplast DNA. Orf38 is located just downstream of the psbE and psbF genes for the polypeptides of cytochrome b-559. Analysis of the transcription of this region of chloroplast DNA shows that psbE, psbF and orf38 are co-transcribed to give a 1.1 kb polycistronic transcript which also contains another open reading frame of 40 codons. The orf38 and orf40 products are hydrophobic polypeptides which are both predicted to span the thylakoid membrane once. Orf38 and orf40 are highly conserved, and map to similar locations adjacent to psbE and psbF, in all organisms from which this region of DNA has been sequenced. We propose that orf38 is named psbL.

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