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Dual targeted poplar ferredoxin NADP+ oxidoreductase interacts with hemoglobin 1

Jokipii-Lukkari, Soile; Kastaniotis, Alexander J.; Parkash, Vimal; Sundström, Robin; Leiva-Eriksson, Nélida LU ; Nymalm, Yvonne; Blokhina, Olga; Kukkola, Eija; Fagerstedt, Kurt V. and Salminen, Tiina A., et al. (2016) In Plant Science 247. p.138-149
Abstract

Previous reports have connected non-symbiotic and truncated hemoglobins (Hbs) to metabolism of nitric oxide (NO), an important signalling molecule involved in wood formation. We have studied the capability of poplar (Populus tremula × tremuloides) Hbs PttHb1 and PttTrHb proteins alone or with a flavin-protein reductase to relieve NO cytotoxicity in living cells. Complementation tests in a Hb-deficient, NO-sensitive yeast (Saccharomyces cerevisiae) δyhb1 mutant showed that neither PttHb1 nor PttTrHb alone protected cells against NO. To study the ability of Hbs to interact with a reductase, ferredoxin NADP+ oxidoreductase PtthFNR was characterized by sequencing and proteomics. To date, by far the greatest number of the known... (More)

Previous reports have connected non-symbiotic and truncated hemoglobins (Hbs) to metabolism of nitric oxide (NO), an important signalling molecule involved in wood formation. We have studied the capability of poplar (Populus tremula × tremuloides) Hbs PttHb1 and PttTrHb proteins alone or with a flavin-protein reductase to relieve NO cytotoxicity in living cells. Complementation tests in a Hb-deficient, NO-sensitive yeast (Saccharomyces cerevisiae) δyhb1 mutant showed that neither PttHb1 nor PttTrHb alone protected cells against NO. To study the ability of Hbs to interact with a reductase, ferredoxin NADP+ oxidoreductase PtthFNR was characterized by sequencing and proteomics. To date, by far the greatest number of the known dual-targeted plant proteins are directed to chloroplasts and mitochondria. We discovered a novel variant of hFNR that lacks the plastid presequence and resides in cytosol. The coexpression of PttHb1 and PtthFNR partially restored NO resistance of the yeast δyhb1 mutant, whereas PttTrHb coexpressed with PtthFNR failed to rescue growth. YFP fusion proteins confirmed the interaction between PttHb1 and PtthFNR in plant cells. The structural modelling results indicate that PttHb1 and PtthFNR are able to interact as NO dioxygenase. This is the first report on dual targeting of central plant enzyme FNR to plastids and cytosol.

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published
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keywords
Dioxygenation, Dual targeting, Ferredoxin NADP oxidoreductase, Hemoglobin, Nitric oxide, Poplar
in
Plant Science
volume
247
pages
12 pages
publisher
Elsevier
external identifiers
  • Scopus:84962714447
ISSN
0168-9452
DOI
10.1016/j.plantsci.2016.03.013
language
English
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yes
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a57a59f4-db3d-4dc2-aaa3-be935b71a811
date added to LUP
2016-04-29 13:56:04
date last changed
2016-10-11 14:09:38
@misc{a57a59f4-db3d-4dc2-aaa3-be935b71a811,
  abstract     = {<p>Previous reports have connected non-symbiotic and truncated hemoglobins (Hbs) to metabolism of nitric oxide (NO), an important signalling molecule involved in wood formation. We have studied the capability of poplar (Populus tremula × tremuloides) Hbs PttHb1 and PttTrHb proteins alone or with a flavin-protein reductase to relieve NO cytotoxicity in living cells. Complementation tests in a Hb-deficient, NO-sensitive yeast (Saccharomyces cerevisiae) δyhb1 mutant showed that neither PttHb1 nor PttTrHb alone protected cells against NO. To study the ability of Hbs to interact with a reductase, ferredoxin NADP<sup>+</sup> oxidoreductase PtthFNR was characterized by sequencing and proteomics. To date, by far the greatest number of the known dual-targeted plant proteins are directed to chloroplasts and mitochondria. We discovered a novel variant of hFNR that lacks the plastid presequence and resides in cytosol. The coexpression of PttHb1 and PtthFNR partially restored NO resistance of the yeast δyhb1 mutant, whereas PttTrHb coexpressed with PtthFNR failed to rescue growth. YFP fusion proteins confirmed the interaction between PttHb1 and PtthFNR in plant cells. The structural modelling results indicate that PttHb1 and PtthFNR are able to interact as NO dioxygenase. This is the first report on dual targeting of central plant enzyme FNR to plastids and cytosol.</p>},
  author       = {Jokipii-Lukkari, Soile and Kastaniotis, Alexander J. and Parkash, Vimal and Sundström, Robin and Leiva-Eriksson, Nélida and Nymalm, Yvonne and Blokhina, Olga and Kukkola, Eija and Fagerstedt, Kurt V. and Salminen, Tiina A. and Läärä, Esa and Bülow, Leif and Ohlmeier, Steffen and Hiltunen, J. Kalervo and Kallio, Pauli T. and Häggman, Hely},
  issn         = {0168-9452},
  keyword      = {Dioxygenation,Dual targeting,Ferredoxin NADP oxidoreductase,Hemoglobin,Nitric oxide,Poplar},
  language     = {eng},
  month        = {06},
  pages        = {138--149},
  publisher    = {ARRAY(0xd2b20e8)},
  series       = {Plant Science},
  title        = {Dual targeted poplar ferredoxin NADP<sup>+</sup> oxidoreductase interacts with hemoglobin 1},
  url          = {http://dx.doi.org/10.1016/j.plantsci.2016.03.013},
  volume       = {247},
  year         = {2016},
}