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cytidine/mais

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ArtiklidKliinilistes uuringutesPatendid
13 tulemused
Enzymatic proteins with deoxycytidine and cytidine aminohydrolase activities were partially purified from Zea mays L. aerial parts by using ammonium sulfate fractionation, adsorption on calcium phosphate gel and chromatography on DEAE-cellulose.
Phosphatidylinositol (PtdIns) is an important lipid because it serves as a key membrane constituent and is the precursor of the inositol-containing lipids that are found in all plants and animals. It is synthesized from cytidine-diphosphodiacylglycerol (CDP-DG) and myo-inositol by PtdIns synthase
RNA editing modifies cytidines (C) to uridines (U) at specific sites in the transcripts of mitochondria and plastids, altering the amino acid specified by the DNA sequence. Here we report the identification of a critical editing factor of mitochondrial nad7 transcript via molecular characterization

Precise base editing in rice, wheat and maize with a Cas9-cytidine deaminase fusion.

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Targeted base editing in plants without the need for a foreign DNA donor or double-stranded DNA cleavage would accelerate genome modification and breeding in a wide array of crops. We used a CRISPR-Cas9 nickase-cytidine deaminase fusion to achieve targeted conversion of cytosine to thymine from

Non-allosteric regulation of the uridine kinase from seeds of Zea mays.

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Uridine kinase (ATP: uridine 5'-phosphotransferase, EC 2.7.1.48) has been partially purified from ungerminated hybrid corn seed. It is associated with a soluble high molecular weight fraction from which it apparently cannot be dissociated without loss of activity. The stability of the enzyme is

Cytochemical studies concerning the occurrence and distribution of RNA in plastids of Zea mays.

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The occurrence of RNA in plastids from etiolated and green maize leaves was demonstrated cytochemically, with both the light and the electron microscope. Etiolated leaves were allowed to incorporate tritiated cytidine for several hours and were subsequently fixed in formalin. Radioautographs of leaf
When green leaves of spinach (Spinacia oleracea L.) were surveyed for the presence of hexokinases which utilize glucose, fructose and-or mannose as a substrate, four kinases could be distinguished by their order of elution during chromatography on diethylaminoethyl (DEAE)-cellulose: (i) a hexokinase

Citrate synthetase in mitochondria and glyoxysomes of maize scutellum.

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Mitochondria and glyoxysomes were isolated from scutella of maize (Zea mays L.) by density gradient centrifugation. Citrate synthetase was partly solubilized from the organelles by sonication. The sonicated organelle suspensions were centrifuged at high speed, and the supernatants were used as
A computational analysis of RNA editing sites was performed on protein-coding sequences of plant mitochondrial genomes from Arabidopsis thaliana, Beta vulgaris, Brassica napus, and Oryza sativa. The distribution of nucleotides around edited and unedited cytidines was compared in 41 nucleotide

The RNA editing factor SlORRM4 is required for normal fruit ripening in tomato.

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RNA editing plays a key posttranscriptional role in gene expression. Existing studies on cytidine-to-uridine RNA editing in plants have focused on maize (Zea mays), rice (Oryza sativa), and Arabidopsis (Arabidopsis thaliana). However, the importance and regulation of RNA editing in several critical
RNA editing, converting cytidines (C) to uridines (U) at specific sites in the transcripts of mitochondria and plastids, plays a critical role in organelle gene expression in land plants. Recently pentatricopeptide repeat (PPR) proteins were identified as site-specific recognition factors for RNA
In flowering plants, RNA editing is a posttranscriptional mechanism that converts specific cytidines to uridines in both mitochondrial and plastidial transcripts, altering the information encoded by these genes. Here, we report the molecular characterization of the empty pericarp5 (emp5) mutants in
RNA editing plays an important role in organellar gene expression in plants, and pentatricopeptide repeat (PPR) proteins are involved in this function. Because of its large family size, many PPR proteins are not known for their function and roles in plant growth and development. Through genetic and
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