Homology of the N-terminal domain of the petH gene product from Anabaena sp. PCC 7119 to the CpcD phycobilisome linker polypeptide |
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Authors: | M. F. Fillat E. Flores C. Gómez-Moreno |
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Affiliation: | (1) Departamento de Bioquímica y Biología Molecular y Celular, Universidad de Zaragoza, 50009 Zaragoza, Spain;(2) Instituto de Bioquímica Vegetal y Fotosíntesis, CSIC, Universidad de Sevilla, Apartado 1113, 41080 Sevilla, Spain |
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Abstract: | The complete nucleotide sequence of the petH gene encoding ferredoxin-NADP+ reductase from the nitrogen-fixing cyanobacterium Anabaena sp. PCC 7119 has been determined. The encoded polypeptide is 136 amino acids longer than the enzyme obtained after purification to homogeneity. The extended N-terminal domain consists of 80 amino acids which shows homology to the CpcD phycobilisome linker polypeptide, through which FNR might be anchored to the thylakoid-bound phycobilisomes. A 56 amino acid interdomain fragment is found which could be a target for proteolysis. |
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Keywords: | Anabaena sp. CpcD-like domain ferredoxin-NADP+ reductase petH |
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