4.5 Article

Effect of salinity on ccmfn gene RNA editing of mitochondria in wild barley and uncommon types of RNA editing

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FUNCTIONAL & INTEGRATIVE GENOMICS
卷 23, 期 1, 页码 -

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SPRINGER HEIDELBERG
DOI: 10.1007/s10142-023-00978-5

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RNA editing; Ccmfn; Wild barley; Salinity stress

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The mitochondria are responsible for cellular respiration and energy production. The Cytochrome C complex plays a crucial role in electron transport between complex III and complex IV in the respiratory chain. One of the main subunits of this complex, CcmFN, is believed to be essential for assembling holocytochrome. In the wild-type plant Hordeum vulgare subsp. spontaneum, the ccmfn gene is subjected to high salt stress, resulting in various nucleotide and amino acid modifications. The study also discovered unusual RNA editing types, such as A to C, C to A, A to G, A to U, T to A, T to C, C to G, G to C, and T to G, which differ from typical C to U editing observed in most cases.
The primary function of mitochondria is cellular respiration and energy production. Cytochrome C complex is an essential complex that transports electrons in the respiratory chain between complex III and complex IV. One of this complex's main subunits is CcmFN, which is believed to be crucial for holocytochrome assembly. In wild-type plant Hordeum vulgare subsp. spontaneum, four ccmfn cDNAs are subjected to high salt stress (500 mM salinity), 0 h (or control) (GenBank accession no. ON764850), after 2 h (GenBank accession no. ON7648515), after 12 h (GenBank accession no. ON764852), and after 24 h (GenBank accession no. ON764853) and mtDNA of ccmfn gene (GenBank accession no. ON764854). Using raw data from RNA-seq, 47 sites with nucleotide and amino acid modifications were detected. There were ten different RNA editing types, with most of them are C to U. Unusual editing types in plants have also been found, such as A to C, C to A, A to G, A to U, T to A, T to C, C to G, G to C, and T to G. High levels of editing were observed in control as well as treatments of salinity stress. Amino acid changes were found in 43 sites; nearly all showed hydrophilic to hydrophilic alterations. Only C749 showed regulation under salinity stress.

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