Proteomic survey of metabolic pathways in rice
Top Cited Papers
Open Access
- 5 August 2002
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 99 (18) , 11969-11974
- https://doi.org/10.1073/pnas.172183199
Abstract
A systematic proteomic analysis of rice ( Oryza sativa ) leaf, root, and seed tissue using two independent technologies, two-dimensional gel electrophoresis followed by tandem mass spectrometry and multidimensional protein identification technology, allowed the detection and identification of 2,528 unique proteins, which represents the most comprehensive proteome exploration to date. A comparative display of the expression patterns indicated that enzymes involved in central metabolic pathways are present in all tissues, whereas metabolic specialization is reflected in the occurrence of a tissue-specific enzyme complement. For example, tissue-specific and subcellular compartment-specific isoforms of ADP-glucose pyrophosphorylase were detected, thus providing proteomic confirmation of the presence of distinct regulatory mechanisms involved in the biosynthesis and breakdown of separate starch pools in different tissues. In addition, several previously characterized allergenic proteins were identified in the seed sample, indicating the potential of proteomic approaches to survey food samples with regard to the occurrence of allergens.Keywords
This publication has 55 references indexed in Scilit:
- Functional architecture of the major light-harvesting complex from higher plantsJournal of Molecular Biology, 2001
- Contemplating the End of the BeginningGenome Research, 2001
- ChloroP, a neural network‐based method for predicting chloroplast transit peptides and their cleavage sitesProtein Science, 1999
- Identification of gel-separated proteins by liquid chromatography-electrospray tandem mass spectrometry: Comparison of methods and their limitationsElectrophoresis, 1998
- Classification of rice allergenic protein cDNAs belonging to the α-amylase/trypsin inhibitor gene familyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein databaseJournal of the American Society for Mass Spectrometry, 1994
- SORTEZ: a relational translator for NCBI's ASN.1 databaseBioinformatics, 1994
- Basic Local Alignment Search ToolJournal of Molecular Biology, 1990
- Basic local alignment search toolJournal of Molecular Biology, 1990