ArticleMolecular biology reports2014
Profiling of mitochondrial proteome in wheat roots.
Article in Molecular biology reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Crop Proteomics under Abiotic Stress: From Data to Insights.Plants (Basel, Switzerland) · 2022Review
- Wheat Proteomics for Abiotic Stress Tolerance and Root System Architecture: Current Status and Future Prospects.Proteomes · 2022Review
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondria are important organelles for cellular respiration within the eukaryotic cell and have many important functions including vitamin synthesis, amino acid metabolism and photorespiration. To investigate the mitochondrial proteome of the roots of wheat seedlings, a systematic and targeted analysis were carried out on the mitochondrial proteome from 15 day-old wheat seedling root material. Mitochondria were isolated by Percoll gradient centrifugation; and extracted proteins were disassociated and analyzed by Tricine SDS-PAGE couple to LTQ-FTICR mass spectrometry. From the isolated the sample, 184 proteins were identified which is composed of 140 proteins as mitochondria and 44 proteins as other subcellular proteins that are predicted by the freeware sub-cellular predictor. The identified proteins in mitochondria were functionally classified into 12 classes using the ProtFun 2.2 servers based on biological processes. Proteins were shown to be involved in amino acid biosynthesis (17.1%), biosynthesis of cofactors (6.4%), cell envelope (11.4%), central intermediary metabolism (10%), energy metabolism (20%), fatty acid metabolism (0.7%), purines and pyrimidines (5.7%), regulatory functions (0.7%), replication and transcription (1.4%), translation (22.1%), transport and binding (1.4%), and unknown (2.8%). These results indicate that many of the protein components present and functions of identifying proteins are common to other profiles of mitochondrial proteins performed to date. These results are provided the extensive and noble clues, to our knowledge, of mitochondrial proteins from wheat roots.
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