کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8299199 | 1537052 | 2008 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Biogenesis of cytochrome c oxidase - in vitro approaches to study cofactor insertion into a bacterial subunit I
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کلمات کلیدی
EXAFSParacoccus denitrificansHeme aBCATXRFIMSCMCCOXimm - انحصارTev - به توCell-free expression - بیان سلولی آزادinner mitochondrial membrane - درونی غشای میتوکندریSubunit - زیرمجموعهextended X-ray absorption fine structure - ساختار ریز جذب جذب اشعه ایکسcytochrome c oxidase - سیتوکروم سی اکسیدازCopper chaperone - شاپور مسcritical micelle concentration - غلظت متیل مهمintermembrane space - فضای بین محوریAssembly - مونتاژTobacco etch virus - ویروس تنباکو اچTotal reflection X-ray fluorescence - کل بازتاب اشعه ایکس اشعه ماوراء بنفش
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Biogenesis of cytochrome c oxidase is a complex process involving more than 30 known accessory proteins in yeast for the regulation of transcription and translation, membrane insertion and protein processing, cofactor insertion, and subunit assembly. Here, we focus on the process of cofactor insertion into subunit I of cytochrome c oxidase using the soil bacterium Paracoccus denitrificans as a model organism. The use of bacterial systems facilitates biogenesis studies, as the number of required assembly factors is reduced to a minimum. Both, co- and posttranslational cofactor insertion scenarios are discussed, and several approaches to shed light on this aspect of biogenesis are presented. CtaG, the Paracoccus homolog of yeast Cox11 which is involved in copper delivery to the CuB center, has been purified and characterized spectroscopically. A previously unreported signal at 358Â nm allows monitoring copper transfer from copper-loaded CtaG to an acceptor. Both CtaG and apo-subunit I were purified after expression in Escherichia coli to develop an in vitro copper transfer system, probing the posttranslational insertion hypothesis. To mimic a potential cotranslational insertion process, cell-free expression systems using E. coli and P. denitrificans extracts have been established. Expression of subunit I in the presence of the detergent Brij-35 produces high amounts of “solubilized” subunit I which can be purified in good yield. With this system it may be feasible to trap and purify assembly intermediates after adding free cofactors, purified assembly proteins, or P. denitrificans membranes.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1777, Issues 7â8, JulyâAugust 2008, Pages 904-911
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1777, Issues 7â8, JulyâAugust 2008, Pages 904-911
نویسندگان
Peter Greiner, Achim Hannappel, Carolin Werner, Bernd Ludwig,