کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2016949 | 1542042 | 2016 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Dual targeted poplar ferredoxin NADP+ oxidoreductase interacts with hemoglobin 1
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
non-symbiotic hemoglobinHBSBiFC2-DEPMFnsHbORFDETA NONOateNOD(Z)-1-[N-(2-aminoethyl)-N-(2-ammonioethyl)amino]diazen-1-ium-1,2-diolatePeptide mass fingerprint - اثر انگشت پپتیدهtwo-dimensional gel electrophoresis - الکتروفورز ژل دو بعدیDioxygenation - اکسیژنزداییrapid amplification of cDNA ends - تقویت سریع cDNA به پایان می رسدbimolecular fluorescence complementation - تکمیل فلورسانس دو طرفه حرکتیdigoxigenin - دیگوکسین ژنDIG - شماPoplar - صنوبرMass spectrometry - طیف سنجی جرمیopen reading frame - قاب خواندن بازPipes - لوله هایRace - مسابقهwild-type - نوع وحشیsodium nitroprusside - نیتروپروساید سدیمNitric oxide - نیتریک اکسیدDual targeting - هدف دوگانهHemoglobin - هموگلوبینTruncated hemoglobin - هموگلوبین مختصرHemoglobins - هموگلوبین هاSNP - چندریختی تک-نوکلئوتید
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
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 Ã 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) Îyhb1 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 Îyhb1 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Science - Volume 247, June 2016, Pages 138-149
Journal: Plant Science - Volume 247, June 2016, Pages 138-149
نویسندگان
Soile Jokipii-Lukkari, Alexander J. Kastaniotis, Vimal Parkash, Robin Sundström, Nélida Leiva-Eriksson, Yvonne Nymalm, Olga Blokhina, Eija Kukkola, Kurt V. Fagerstedt, Tiina A. Salminen, Esa Läärä, Leif Bülow, Steffen Ohlmeier, J. Kalervo Hiltunen,