کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2016777 | 1067687 | 2009 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
BN-PAGE analysis of the respiratory chain complexes in mitochondria of cucumber MSC16 mutant
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
NADH–ubiquinone oxidoreductasePVPDTTMOPSOXPHOSBN-PAGEAOXCMSNCS4-morpholinepropanesulfonic acid - 4-مورفولین پروپان سولفونیک اسیدBSA - BSAbovine serum albumin - آلبومین سرم گاوCytoplasmic male sterile - استریل مرد سیتوپلاسمیblue-native polyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمید آبی بومیAlternative oxidase - اکسیداز جایگزینsuccinate dehydrogenase - سوکسیناد دهیدروژنازOxidative phosphorylation - فسفوریلاسیون اکسیداتیوComplex I - مجتمع IComplex IV - مجتمع IVComplex II - مجتمع دومwild-type - نوع وحشیcomplex III - پیچیده III
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Rearrangements of mitochondrial DNA in MSC16 mutant of cucumber (Cucumis sativus L.) affect mitochondrial functioning due to the alteration mainly of Complex I resulting in several metabolic changes. One-dimensional Blue-Native polyacrylamide gel electrophoresis (BN-PAGE) and densitometric measurements showed that the level and in-gel capacity of Complex I were lower in MSC16 leaf and root mitochondria as compared to wild-type (WT). The level and capacity of supercomplex IÂ +Â III2 were always lower in leaf but not in MSC16 root mitochondria. Two-dimensional BN/SDS-PAGE indicated that the band abundance for most of the subunits of Complex I was lower in MSC16 leaf and root mitochondria. Supercomplex IÂ +Â III2 level was only altered in MSC16 leaf mitochondria as measured after 2D BN/SDS-PAGE. No differences in the qualitative composition of the subunits of Complex I and supercomplex IÂ +Â III2 between MSC16 and WT mitochondria were observed. In MSC16 mitochondria Complex I impairment could be compensated to some extent by additional respiratory chain NADH dehydrogenases. A higher capacity and level of NDB-1 protein of external NADH dehydrogenase was observed in MSC16 leaf and root mitochondria as compared to WT. The level of COX II, mitochondrial-encoded subunit of Complex IV, was higher in MSC16 leaf and root mitochondria. However, the capacity of Complex IV was slightly higher only in MSC16 leaf mitochondria. The levels of complexes: III2 and V and Complex V capacity did not differ in mitochondria between genotypes. An abundance of the subunits of respiratory complexes is one of the key factors determining not only their structure and functional stability but also a formation of the supercomplexes. We discuss here mitochondrial genome rearrangements in MSC16 mutant in a relation to assembly and/or stability (the lower level and capacity) of Complex I and supercomplex IÂ +Â III2.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Physiology and Biochemistry - Volume 47, Issue 5, May 2009, Pages 397-406
Journal: Plant Physiology and Biochemistry - Volume 47, Issue 5, May 2009, Pages 397-406
نویسندگان
Izabela M. Juszczuk, Anna M. Rychter,