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Examination of protein sequence homologies: V. New perspectives on evolution between bacterial and chloroplast-type ferredoxins inferred from sequence evidence

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Summary

Sequence homologies among 34 chloroplast-type ferredoxins were examined using a computer program that quantitatively evaluates the extent of sequence similarity as a correlation coefficient. The resultant alignment contains six gaps representing insertions or deletions of some residues, all of which are located such that they precisely preserve the domains of structural fragments as determined by crystallographic data onSpirulina platensis ferredoxin.

In the search for any total correlation between the chloroplast-type and 27 bacterial ferredoxins, 1891 comparison matrices prepared for possible combinations indicated that the bacterial basal sequence of 55 residues has been conserved evolutionarily in the chloroplast-type sequences corresponding to residue positions 36–90 ofSpirulina platensis ferredoxin. In addition, the bacterial “connector sequence” region was found to be conserved. These findings strongly suggest that the bacterial and chloroplast-type ferredoxins descended from a common ancestor, and branched off after the bacterial gene duplication, whereas the chloroplast-type ferredoxins originally were generated by duplicating the already duplicated bacterial gene, i.e., by “double-duplication.”

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References

  • Adman ET, Sieker LC, Jensen LH (1973) The structure of bacterial ferredoxin. J Biol Chem 248:3987–3996

    PubMed  Google Scholar 

  • Benson AM, Yasunobu KT (1969) Non-heme iron proteins. X. The amino acid sequences of ferredoxins fromLeucaena glauca. J Biol Chem 244:955–963

    PubMed  Google Scholar 

  • Borden D, Margoliash E (1979) Taken from NBRF file. [In: Cades JS (1977) The primary structures of the ferredoxin and the cytochromef from a blue-green alga,Synechococcus lividus. PhD thesis, Northwestern University, Evanston IL]

    Google Scholar 

  • Eck RV, Dayhoff MO (1966) Evolution of the structure of ferredoxin based on living relics of primitive amino acid sequences. Science 152:363–366

    Google Scholar 

  • Fukuyama K, Hase T, Matsumoto S, Tsukihara T, Katsube Y, Tanaka N, Kakudo M, Wada K, Matsubara H (1980) Structure ofS. platensis [2Fe−2S] ferredoxin and evolution of chloroplast-type ferredoxins. Nature 286:522–524

    Google Scholar 

  • George DG, Hunt LT, Yeh LL, Barker WC (1985) New perspectives on bacterial ferredoxin evolution. J Mol Evol 22: 20–31

    PubMed  Google Scholar 

  • Hase T, Wada K, Matsubara H (1976a) Amino acid sequence of the major component ofAphanothece sacrum ferredoxin. J Biochem 79:329–343

    PubMed  Google Scholar 

  • Hase T, Wada K, Ohmiya M, Matsubara H (1976b) Amino acid sequence of the major component ofNostoc muscorum ferredoxin. J Biochem 80:993–999

    PubMed  Google Scholar 

  • Hase T, Wada K, Matsubara H (1977) Horsetail (Equisetum telmateia) ferredoxins I and II. Amino acid sequences. J Biochem 82:267–276

    PubMed  Google Scholar 

  • Hase T, Wakabayashi S, Matsubara H, Kerscher L, Oesterhelt D, Rao KK, Hall DO (1978a) Complete amino acid sequence ofHalobacterium halobium ferredoxin containing an N-acetyllysine residue. J Biochem 83:1657–1670

    PubMed  Google Scholar 

  • Hase T, Wakabayashi S, Matsubara H, Rao KK, Hall DO, Widmer H, Gysi J, Zuber H (1978b) The amino acid sequence of ferredoxin from the algaMastigocladus laminosus. Phytochemistry 17:1863–1867

    Article  Google Scholar 

  • Hase T, Wakabayashi S, Wada K, Matsubara H (1978c) Amino acid sequence ofAphanothece sacrum ferredoxin II (minor component). Structural characteristics and evolutionary implications. J Biochem 83:761–770

    PubMed  Google Scholar 

  • Hase T, Wakabayashi S, Wada K, Matsubara H, Juttner F, Rao KK, Fry I, Hall DO (1978d)Cyanidium caldarium ferredoxin: a red algal type. FEBS Lett 96:41–44

    Article  Google Scholar 

  • Hase T, Matsubara H, Ben-Amotz A, Rao KK, Hall DO (1980a) Purification and sequence determination of two ferredoxins fromDunaliella salina. Phytochemistry 19:2065–2070

    Article  Google Scholar 

  • Hase T, Wakabayashi S, Matsubara H, Mevarech M, Werber MM (1980b) Amino acid sequence of 2Fe−2S ferredoxin from an extreme halophile,Halobacterium of the dead sea. Biochim Biophys Acta 623:139–145

    PubMed  Google Scholar 

  • Hase T, Inoue K, Matsubara H, Williams MM, Rogers LJ (1982a) Amino acid sequence ofSynechocystis 6714 ferredoxin: a unique structural feature of unicellular blue-green algal ferredoxin. J Biochem 92:1357–1362

    PubMed  Google Scholar 

  • Hase T, Matsubara H, Hutber GN, Rogers LJ (1982b) Amino acid sequence ofNostoc strain MAC ferredoxins I and II. J Biochem 92:1347–1355

    PubMed  Google Scholar 

  • Hase T, Yamanashi H, Matsubara H (1982c) Purification and amino acid sequence of a fern (Gleichenia japonica) ferredoxin. J Biochem 91:341–346

    PubMed  Google Scholar 

  • Howard JB, Lorsbach TW, Ghosh D, Melis K, Stout CD (1983) Structure ofAzotobacter vinelandii 7Fe ferredoxin: amino acid sequence and electron density maps of residues. J Biol Chem 258:508–522

    PubMed  Google Scholar 

  • Keresztes-Nagy S, Perini F, Margoliash E (1969) Primary structure of alfalfa ferredoxin. J Biol Chem 244:981–995

    PubMed  Google Scholar 

  • Kubota Y, Takahashi S, Nishikawa K, Ooi T (1981) Homology in protein expressed by correlation coefficients. J Theor Biol 91:347–361

    Article  PubMed  Google Scholar 

  • Kubota Y, Nishikawa K, Takahashi S, Ooi T (1982) Correspondence of homologies in amino acid sequence and tertiary structure of protein molecules. Biochim Biophys Acta 701: 242–252

    PubMed  Google Scholar 

  • Matsubara H, Sasaki RM, Chain RK (1967) The amino acid sequence of spinach ferredoxin. Proc Natl Acad Sci USA 57: 439–445

    Google Scholar 

  • Otaka E, Ooi T (1987) Examination of protein sequence homologies: IV. Twenty-seven bacterial ferredoxins. J Mol Evol 26:257–267

    Article  PubMed  Google Scholar 

  • Otaka E, Ooi T, Kumazaki T, Itoh T (1985a) Examination of protein sequence homologies: I. ElevenE. coli L7/L12-type ribosomal “A” protein sequences from eubacteria and chloroplast. J Mol Evol 21:339–345

    Google Scholar 

  • Otaka E, Ooi T, Kumazaki T, Itoh T (1985b) Examination of protein sequence homologies: II. SixE. coli L7/L12-type ribosomal “A” protein sequences from eukaryotes and metabacteria, contrasted with those from prokaryotes. J Mol Evol 22:342–350

    Google Scholar 

  • Otaka E, Ooi T, Itoh T, Kumazaki T (1986) Examination of protein sequence homologies: III. Ribosomal protein YS25 fromSaccharomyces cerevisiae and its counterparts fromSchizosaccharomyces pombe, rat liver andEscherichia coli. J Mol Evol 23:337–342

    PubMed  Google Scholar 

  • Rao KK, Matsubara H (1970) The amino acid sequence of taro ferredoxin. Biochem Biophys Res Commun 38:500–508

    Article  PubMed  Google Scholar 

  • Sugeno K, Matsubara H (1969) The amino acid sequence ofScenedesmus ferredoxin. J Biol Chem 244:2979–2989

    PubMed  Google Scholar 

  • Takahashi Y, Hase T, Matsubara H, Hutber GN, Rogers LJ (1982) Amino acid sequence ofChlorogloeopsis fritschii ferredoxin: taxonomic and evolutionary aspects. J Biochem 92: 1363–1368

    PubMed  Google Scholar 

  • Takahashi Y, Hase T, Wada K, Matsubara H (1983) Ferredoxins in developing spinach cotyledons: the presence of two molecular species. Plant Cell Physiol 24:189–198

    Google Scholar 

  • Takruri IAH, Boulter D (1979a) The amino acid sequence of ferredoxin fromSambucus nigra. Phytochemistry 18:1481–1484

    Article  Google Scholar 

  • Takruri IAH, Boulter D (1979b) The amino acid sequence of ferredoxin fromTriticum aestivum (wheat). Biochem J 179: 373–378

    PubMed  Google Scholar 

  • Takruri IAH, Boulter D (1980) The amino acid sequence of ferredoxin fromBrassica napus (rape). Biochem J 185:239–243

    PubMed  Google Scholar 

  • Takruri IAH, Haslett BG, Boulter D, Andrew PW, Rogers LJ (1978) The amino acid sequence of ferredoxin from the red algaPorphyra umbilicalis. Biochem J 173:459–466

    PubMed  Google Scholar 

  • Takruri IAH, Gilroy J, Boulter D (1982) Amino acid sequence of ferredoxin fromArctium lappa. Phytochemistry 21:325–327

    Article  Google Scholar 

  • Tanaka M, Nakashima T, Benson E, Mower H, Yasunobu KT (1966) The amino acid sequence ofClostridum pesteurianum ferredoxin. Biochemistry 5:1665–1681

    Article  Google Scholar 

  • Tanaka M, Haniu M, Yasunobu KT, Rao KK, Hall DO (1975) Modification of the automated sequence determination as applied to the sequence determination of theSpirulina maxima ferredoxin. Biochemistry 14:5535–5540

    Article  PubMed  Google Scholar 

  • Tsukihara T, Katsube Y, Hase T, Wada K, Matsubara H (1982) Evolutionary relationship between [2Fe−2S] ferredoxins and an ancestral ferredoxin. In: Kimura M (ed) Molecular evolution, protein polymorphism and the neutral theory. Japan Scientific Societies Press, Tokyo, and Springer-Verlag, Berlin, pp 299–312

    Google Scholar 

  • Tsukihara T, Fukuyama K, Wakabayashi S, Wada K, Matsubara H, Kerscher L, Oesterhelt D (1985) Preliminary X-ray diffraction studies on a ferredoxin from the thermophilic archaebacteria,Thermoplasma acidophilum. J Mol Biol 186:481–482

    Article  PubMed  Google Scholar 

  • Wada K, Hase T, Tokunaga H, Matsubara H (1975) Amino acid sequence ofSpirulina platensis ferredoxin: a far divergency of blue-green algal ferredoxins. FEBS Lett 55:102–104

    Article  PubMed  Google Scholar 

  • Wakabayashi S, Hase Y, Wada K, Matsubara H, Suzuki K, Takaichi S (1978) Amino acid sequences of two ferredoxins from pokeweed,Phytolacca americana. J Biochem 83:1305–1319

    PubMed  Google Scholar 

  • Wakabayashi S, Hase T, Wada K, Matsubara H, Suzuki K (1980) Amino acid sequences of two ferredoxins fromPhytolacca esculenta. Gene duplication and speciation. J Biochem 87: 227–236

    PubMed  Google Scholar 

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Otaka, E., Ooi, T. Examination of protein sequence homologies: V. New perspectives on evolution between bacterial and chloroplast-type ferredoxins inferred from sequence evidence. J Mol Evol 29, 246–254 (1989). https://doi.org/10.1007/BF02100208

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  • DOI: https://doi.org/10.1007/BF02100208

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