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Location and nucleotide sequence of the gene for cytochrome f in wheat chloroplast DNA

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Summary

The gene for cytochrome f has been located in wheat chloroplast DNA by hybridisation with a 3.3 kbp BglII fragment of pea chloroplast DNA containing the gene for cytochrome f, by in vitro transcription-translation of cloned restriction fragments of wheat chloroplast DNA and by nucleotide sequence analysis. The gene is located 3 kbp from the 3′ end of the gene for the large subunit of ribulose bisphosphate carboxylase and is transcribed from the same DNA strand. Nucleotide sequence analysis reveals an open reading frame of 320 amino acids, of which 285 amino acid residues comprise the mature polypeptide and 35 amino acid residues probably represent an N-terminal signal sequence. The nucleotide sequence of the wheat gene shows 85% homology with the gene for pea cytochrome f.

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References

  • Alt J, Westhoff P, Sears BB, Nelson N, Hurt E, Hauska G, Herrmann RG (1983) Genes and transcripts for the polypeptides of the cytochrome b6/f complex from spinach thylakoid membranes. EMBO J 2:979–986

    Google Scholar 

  • Bonner WM, Laskey RA (1974) A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem 46:83–88

    Google Scholar 

  • Bowman CM, Dyer TA (1982) Purification and analysis of DNA from wheat chloroplasts isolated in non-aqueous media. Anal Biochem 122:108–118

    Google Scholar 

  • Bowman CM, Koller B, Delius H, Dyer TA (1981) A physical map of wheat chloroplast DNA showing the location of the structural genes for the ribosomal RNAs and the large subunit of ribulose 1,5-bisphosphate carboxylase. Mol Gen Genet 183:93–101

    Google Scholar 

  • Chua N-H, Bennoun P (1975) Thylakoid membrane polypeptides of Chlamydomonas reinhardtii: wild-type and mutant strains deficient in Photosystem II reaction center. Proc Natl Acad Sci USA 72:2175–2179

    Google Scholar 

  • Clewell DB, Helinski DR (1969) Supercoiled circular DNA-protein complex in Escherichia coli: purification and induced conversion to open circular DNA form. Proc Natl Acad Sci USA 62:1159–1166

    Google Scholar 

  • Dickerson RE, Timkovich R (1975) Cytochromes c. In: Boyer PD (ed) The enzymes, vol 11. Academic Press, New York, pp 397–547

    Google Scholar 

  • Doherty A, Gray JC (1979) Synthesis of cytochrome f by isolated pea chloroplasts. Eur J Biochem 98:87–92

    Google Scholar 

  • Dretzen G, Bellard M, Sassone-Corsi P, Chambon P (1981) A reliable method for the recovery of DNA fragments from agarose and acrylamide gels. Anal Biochem 112:295–298

    Google Scholar 

  • Garewal HS, Wasserman AR (1972) “Autoreduction” — an unusual property of pure spinach cytochrome f. Biochim Biophys Acta 275:437–441

    Google Scholar 

  • Garewal HS, Stuart AL, Wasserman AR (1974) Autoreduction of pure spinach cytochrome f: a light-dependent process inhibited by 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Can J Biochem 52:67–70

    Google Scholar 

  • Gray JC (1978) Purification and properties of monomeric cytochrome f from charlock, Sinapis arvensis L. Eur J Biochem 82:133–141

    Google Scholar 

  • Gregory P, Bradbeer JW (1973) Plastid development in primary leaves of Phaseolus vulgaris: the light-induced development of the chloroplast cytochromes. Planta 109:317–326

    Google Scholar 

  • Guikema JA, Sherman LA (1980) Electrophoretic profiles of cyanobacterial membrane polypeptides showing heme-dependent peroxidase activity. Biochim Biophys Acta 637:189–201

    Google Scholar 

  • Highfield PE, Ellis RJ (1976) Protein synthesis in chloroplasts VII. Initiation of protein synthesis in isolated intact pea chloroplasts. Biochim Biophys Acta 447:20–27

    Google Scholar 

  • Ho KK, Krogmann DW (1980) Cytochrome f from spinach and cyanobacteria. J Biol Chem 255:3855–3861

    Google Scholar 

  • Howe CJ, Auffret AD, Doherty A, Bowman CM, Dyer TA, Gray JC (1982a) Location and nucleotide sequence of the gene for the proton-translocating subunit of wheat chloroplast ATP synthase. Proc Natl Acad Sci USA 79:6903–6907

    Google Scholar 

  • Howe CJ, Bowman CM, Dyer TA, Gray JC (1982b) Localization of wheat chloroplast genes for the beta and epsilon subunits of ATP synthase. Mol Gen Genet 186:525–530

    Google Scholar 

  • Howe CJ, Bowman CM, Dyer TA, Gray JC (1983) The genes for the alpha and proton-translocating subunits of wheat chloroplast ATP synthase are close together on the same strand of chloroplast DNA. Mol Gen Genet 190:51–55

    Google Scholar 

  • Huttly AK, Gray JC (1984) Localisation of genes for four subunits of ATP synthase in pea chloroplast DNA. Mol Gen Genet, in press

  • Krinner M, Hauska G, Hurt E, Lockau W (1982) A cytochrome f-b 6 complex with plastoquinol-cytochrome c oxidoreductase activity from Anabaena variabilis. Biochim Biophys Acta 681:110–117

    Google Scholar 

  • Laursen RA (1971) Solid-phase Edman degradation. An automatic peptide sequencer. Eur J Biochem 20:89–102

    Google Scholar 

  • Leis JP, Keller EB (1971) N-formylmethionyl-tRNAf of wheat chloroplasts. Its synthesis by a wheat transformylase. Biochemistry 10:889–894

    Google Scholar 

  • Matsuzaki E, Kamimura Y, Yamasaki T, Yakushiji E (1975) Purification and properties of cytochrome f from Brassica komatsuna leaves. Plant Cell Physiol 17:237–246

    Google Scholar 

  • Nelson N, Racker E (1972) Partial resolution of the enzymes catalysing photophosphorylation X. Purification of spinach cytochrome f and its photo-oxidation by resolved photosystem I particles. J Biol Chem 247:3848–3853

    Google Scholar 

  • Oishi KK, Tewari KK (1983) Characterisation of the gene and mRNA of the large subunit of ribulose-1,5-bisphosphate carboxylase in pea plants. Mol Cell Biol 3:587–595

    Google Scholar 

  • Palmer JD, Thompson WF (1982) Chloroplast DNA rearrangements are more frequent when a large inverted repeat sequence is lost. Cell 29:537–550

    Google Scholar 

  • Palva I, Pettersson RF, Kalkinnen N, Lehtovaara P, Sarvas M, Söderlund H, Takkinen K, Kääriäinen L (1981) Nucleotide sequence of the promoter and NH2-terminal signal peptide region of the α-amylase gene from Bacillus amyloliquefaciens. Gene 15:43–51

    Google Scholar 

  • Perlman D, Halvorson HO (1983) A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol 167:391–409

    Google Scholar 

  • Phillips AL, Gray JC (1983) Isolation and characterisation of a cytochrome b-f complex from pea chloroplasts. Eur J Biochem 137:553–560

    Google Scholar 

  • Sanger F, Coulson AR, Barrell BG, Smith AJH, Roe BA (1980) Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol 143:161–178

    Google Scholar 

  • Schwartz Z, Kossel H (1980) The primary structure of 16S rDNA from Zea mays chloroplasts is homologous to E. coli 16S rRNA. Nature 283:739–742

    Google Scholar 

  • Siedow JN, Vickery LE, Palmer G (1980) The nature of the axial ligands of spinach cytochrome f. Arch Biochem Biophys 203:101–107

    Google Scholar 

  • Süss K-H (1976) Identification of chloroplast thylakoid membrane polypeptides: coupling factor of photophosphorylation (CF1) and cytochrome f. FEBS Lett 70:191–196

    Google Scholar 

  • Sutcliffe JG (1978) Complete nucleotide sequence of Escherichia coli plasmid pBR322. Cold Spring Harbor Symp Quant Biol 43:77–90

    Google Scholar 

  • Tanaka K, Takahashi M, Asada K (1978) Isolation of monomeric cytochrome f from Japanese radish and a mechanism of autoreduction. J Biol Chem 253:7397–7403

    Google Scholar 

  • Tohdoh N, Sugiura M (1982) The complete nucleotide sequence of a 16S ribosomal RNA gene from tobacco chloroplasts. Gene 17:213–218

    Google Scholar 

  • von Heijne G (1983) Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 133:17–21

    Google Scholar 

  • Wachter E, Machleidt W, Hofner H, Otto J (1973) Aminopropyl glass and its p-phenylene diisothiocyanate derivative, a new support in solid-phase Edman degradation of peptides and proteins. FEBS Lett 35:97–102

    Google Scholar 

  • Wahl GM, Stern M, Stark GR (1979) Efficient transfer of large DNA fragments from agarose gels to diazobenzyloxymethylpaper and rapid hybridization by using dextran sulphate. Proc Natl Acad Sci USA 76:3683–3687

    Google Scholar 

  • Walker JE, Auffret AD, Carne A, Gurnett A, Hanisch P, Hill D, Saraste M (1982) Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda. Eur J Biochem 123:253–260

    Google Scholar 

  • Willey DL, Huttly AK, Phillips AL, Gray JC (1983) Localization of the gene for cytochrome f in pea chloroplast DNA. Mol Gen Genet 189:85–89

    Google Scholar 

  • Willey DL, Auffret AD, Gray JC (1984) Structure and topology of cytochrome f in pea chloroplast membranes. Cell 36:555–562

    Google Scholar 

  • Zimmerman CL, Appella E, Pisano JJ (1977) Rapid analysis of amino acid phenylthiohydantoins by high-performance liquid chromatography. Anal Biochem 77:569–573

    Google Scholar 

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Communicated by H. Saedler

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Willey, D.L., Howe, C.J., Auffret, A.D. et al. Location and nucleotide sequence of the gene for cytochrome f in wheat chloroplast DNA. Molec. Gen. Genet. 194, 416–422 (1984). https://doi.org/10.1007/BF00425553

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  • DOI: https://doi.org/10.1007/BF00425553

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