Molecular heterogeneity of ferredoxin-NADP+ reductase from spinach leaves

Hasumi, Hideyo; Nagata, Etsuko

doi:10.1016/0006-291x(83)91292-5

Cited by 23 publications

(16 citation statements)

References 15 publications

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“…Such differences suggest that FNR II could be a partially degraded form ofthe native enzyme, FNR I. FNR II, on the other hand, had a somewhat higher diaphorase activity than FNR I. Limited proteolysis of FNR, resulting in physically altered but still fully functional forms, has been reported for spinach leaf preparations (5). The molecular weight of FNR I is very close to that previously reported for unpurified tomato FNR (18).…”

Section: Fnr Purificationsupporting

confidence: 76%

Ferredoxin and Ferredoxin-NADP Reductase from Photosynthetic and Nonphotosynthetic Tissues of Tomato

Green¹,

Yee²,

Buchanan³

et al. 1991

Plant Physiol.

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Section: Fnr Purificationsupporting

confidence: 76%

Ferredoxin and Ferredoxin-NADP Reductase from Photosynthetic and Nonphotosynthetic Tissues of Tomato

Green¹,

Yee²,

Buchanan³

et al. 1991

Plant Physiol.

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“…All species studied showed the majority of activity in one or two major isozymes. These results are consistent with those reported earlier for FNR from barley [3], spinach [5,7,10,11,19] and Anabaena [18]. Tentoxin has recently been shown to prevent the appearance of an active polyphenol oxidase in chloroplasts of tentoxin-treated tobacco seedlings [26].…”

Section: Resultssupporting

confidence: 83%

“…Some FNR isozymes are interconvertible, and differ by ionic composition rather than molecular weight [5,10]. Some isozymes appear to arise by limited proteolysis [11,12,27]. The formation of dimeric combinations of two different monomeric forms should yield at least three distinguishable isozymes upon electrophoretic separation [16].…”

Section: Resultsmentioning

confidence: 99%

Ferredoxin-NADP+ reductase, a nuclearly-coded enzyme unaffected by tentoxin treatment

et al. 1985

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Previous studies in our laboratory have shown that tentoxin prevents the incorporation of polyphenol oxidase (PPO), a nuclearly-coded protein, into the chloroplasts of sensitive species. In this study, we show, by comparison of electrophoretically separated isozymes, that ferredoxin-NADP(+) reductase (FNR) is nuclearly coded in Nicotiana. Electrophoresis of FNR isozymes from tentoxin treated seedlings of a sensitive and a resistant species demonstrated that, unlike PPO, ferredoxin-NADP(+) reductase was unaffected by tentoxin treatment. These data indicate that tentoxin selectively inhibits transport of cytoplasmically synthesized proteins into the chloroplast, and does not produce a generalized disruption of cellular integration.

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“…It is found as a monomer in the organelle stroma and at the periphery of thylakoid membranes (Berzborn 1968;B6hme 1977;Jennings et al 1979;Clark et al 1984), and has been resolved into several variants or isozyme forms. The significance of these forms, if any, in the different catalytic functions that have been attributed to this enzyme has not yet been elucidated (S~s 1979;Ellefson and Krogmann 1979;Gozzer et al 1977;Hasumi et al 1983;Takahashi et al 1983; see also Zanetti and Curti 1980). Partial solubilization of electrostatically bound FNR from spinach and lettuce thylakoid membranes indicates a photo-regulated interaction with an intrinsic 17.5 kDa polypeptide (Carrillo and Vallejos 1983;Vallejos et al 1984Vallejos et al , 1987Ceccarelli et al 1985;Shin et al 1985;Matthijs et al 1986;Chanet al 1987).…”

Section: Introductionmentioning

confidence: 92%

Analysis of cDNA clones encoding the entire precursor-polypeptide for ferredoxin: NADP+ oxidoreductase from spinach

et al. 1988

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In this paper, we report the structural characterization of several spinach ferredoxin-NADP+ oxidoreductase (FNR) cDNAs ranging in size from 0.9 to 1.5 kilobases. A comparison of the deduced amino acid sequence with the known amino acid sequence determined for the spinach protein establishes that 1.4-1.5 kpb inserts span the full length of the mature protein (314 amino acid residues; Mr = 35,382). These also include an N-terminal 55 amino acid transit peptide as well as maximally 171 and 214 nucleotide 5' and 3' untranslated sequences, respectively. Evidence has been obtained that various forms of FNR arise from at least two similar genes. The FNR precursor (369 amino acid residues) has a calculated molecular mass of 41.2 kDa. Comparison of the transit peptide with transit peptides from two other stromal proteins shows little similarity at the level of primary sequence but some common features in secondary structure predictions.

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Molecular heterogeneity of ferredoxin-NADP+ reductase from spinach leaves

Cited by 23 publications

References 15 publications

Ferredoxin and Ferredoxin-NADP Reductase from Photosynthetic and Nonphotosynthetic Tissues of Tomato

Ferredoxin and Ferredoxin-NADP Reductase from Photosynthetic and Nonphotosynthetic Tissues of Tomato

Ferredoxin-NADP+ reductase, a nuclearly-coded enzyme unaffected by tentoxin treatment

Analysis of cDNA clones encoding the entire precursor-polypeptide for ferredoxin: NADP+ oxidoreductase from spinach

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