共查询到20条相似文献,搜索用时 31 毫秒
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The E domains of pentatricopeptide repeat proteins from different organelles are not functionally equivalent for RNA editing 总被引:1,自引:0,他引:1
Anne‐Laure Chateigner‐Boutin Catherine Colas des Francs‐Small Sota Fujii Kenji Okuda Sandra K. Tanz Ian Small 《The Plant journal : for cell and molecular biology》2013,74(6):935-945
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Anja Zehrmann Barbara H?rtel Franziska Glass Eszter Bayer-Császár Toshihiro Obata Etienne Meyer Axel Brennicke Mizuki Takenaka 《The Journal of biological chemistry》2015,290(10):6445-6456
RNA editing in plastids and mitochondria of flowering plants requires pentatricopeptide repeat proteins (PPR proteins) for site recognition and proteins of the multiple organellar RNA editing factor (MORF) family as cofactors. Two MORF proteins, MORF5 and MORF8, are dual-targeted to plastids and mitochondria; two are targeted to plastids, and five are targeted to mitochondria. Pulldown assays from Arabidopsis thaliana tissue culture extracts with the mitochondrial MORF1 and the plastid MORF2 proteins, respectively, both identify the dual-targeted MORF8 protein, showing that these complexes can assemble in the organelles. We have now determined the scope of potential interactions between the various MORF proteins by yeast two-hybrid, in vitro pulldown, and bimolecular fluorescence complementation assays. The resulting MORF-MORF interactome identifies specific heteromeric MORF protein interactions in plastids and in mitochondria. Heteromers are observed for MORF protein combinations affecting a common site, suggesting their functional relevance. Most MORF proteins also undergo homomeric interactions. Submolecular analysis of the MORF1 protein reveals that the MORF-MORF protein connections require the C-terminal region of the central conserved MORF box. This domain has no similarity to known protein modules and may form a novel surface for protein-protein interactions. 相似文献
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An evolutionarily conserved P‐subfamily pentatricopeptide repeat protein is required to splice the plastid ndhA transcript in the moss Physcomitrella patens and Arabidopsis thaliana
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Ayaka Ito Chieko Sugita Mizuho Ichinose Yoshinobu Kato Hiroshi Yamamoto Toshiharu Shikanai Mamoru Sugita 《The Plant journal : for cell and molecular biology》2018,94(4):638-648
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Barbara Härtel Anja Zehrmann Daniil Verbitskiy Johannes A. van der Merwe Axel Brennicke Mizuki Takenaka 《Plant molecular biology》2013,81(4-5):337-346
A forwards genetic screen of a chemically mutated plant population identified mitochondrial RNA editing factor 10 (MEF10) in Arabidopsis thaliana. MEF10 is a trans-factor required specifically for the C to U editing of site nad2-842. The MEF10 protein is characterized by a stretch of pentatricopeptide repeats (PPR) and a C-terminal extension domain ending with the amino acids DYW. Editing is lost in mutant plants but is recovered by transgenic introduction of an intact MEF10 gene. The MEF10 protein interacts with multiple organellar RNA editing factor 8 (MORF8) but not with other mitochondrial MORF proteins in yeast two hybrid assays. These results support the model that specific combinations of MORF and MEF proteins are involved in RNA editing in plant mitochondria. 相似文献
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Ayoub Bouchoucha Florent Waltz Graldine Bonnard Mathilde Arriv Philippe Hammann Lauriane Kuhn Cdric Schelcher Hlne Zuber Anthony Gobert Philippe Gieg 《The Plant journal : for cell and molecular biology》2019,100(3):549-561
The essential type of endonuclease that removes 5′ leader sequences from transfer RNA precursors is called RNase P. While ribonucleoprotein RNase P enzymes containing a ribozyme are found in all domains of life, another type of RNase P called ‘PRORP’, for ‘PROtein‐only RNase P’, is composed of protein that occurs only in a wide variety of eukaryotes, in organelles and in the nucleus. Here, to find how PRORP functions integrate with other cell processes, we explored the protein interaction network of PRORP1 in Arabidopsis mitochondria and chloroplasts. Although PRORP proteins function as single subunit enzymes in vitro, we found that PRORP1 occurs in protein complexes and is present in high‐molecular‐weight fractions that contain mitochondrial ribosomes. The analysis of immunoprecipitated protein complexes identified proteins involved in organellar gene expression processes. In particular, direct interaction was established between PRORP1 and MNU2 a mitochondrial nuclease. A specific domain of MNU2 and a conserved signature of PRORP1 were found to be directly accountable for this protein interaction. Altogether, results revealed the existence of an RNA maturation complex in Arabidopsis mitochondria and suggested that PRORP proteins cooperated with other gene expression factors for RNA maturation in vivo. 相似文献
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Emp10 encodes a mitochondrial PPR protein that affects the cis‐splicing of nad2 intron 1 and seed development in maize
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Manjun Cai Shuzhen Li Feng Sun Qin Sun Hailiang Zhao Xuemei Ren Yanxin Zhao Bao‐Cai Tan Zuxin Zhang Fazhan Qiu 《The Plant journal : for cell and molecular biology》2017,91(1):132-144
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The Restorer‐of‐fertility‐like 2 pentatricopeptide repeat protein and RNase P are required for the processing of mitochondrial orf291 RNA in Arabidopsis
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Sota Fujii Takamasa Suzuki Philippe Giegé Tetsuya Higashiyama Nobuya Koizuka Toshiharu Shikanai 《The Plant journal : for cell and molecular biology》2016,86(6):504-513
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Yan-Zhuo Yang Shuo Ding Xin-Yuan Liu Chunhui Xu Feng Sun Bao-Cai Tan 《植物学报(英文版)》2023,65(11):2456-2468
RNA helicases participate in nearly all aspects of RNA metabolism by rearranging RNAs or RNA–protein complexes in an adenosine triphosphatedependent manner. Due to the large RNA helicase families in plants, the precise roles of many RNA helicases in plant physiology and development remain to be clarified. Here, we show that mutations in maize(Zea mays) DEAD-box RNA helicase48(Zm RH48) impair the splicing of mitochondrial introns, mitochondrial complex biosynthesis,and seed development. Loss of Z... 相似文献
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