Functional consequences of mitochondrial proteome heterogeneity Export

@article{citeulike:2246744, abstract = {Potential functional consequences of the differences in protein distribution between the mitochondria of the rat liver, heart, brain, and kidney, as determined in the companion paper in this issue (Johnson DT, French S, Blair PV, You JS, Bemis KG, Wang M, Harris RA, and Balaban RS. The tissue heterogeneity of the mammalian mitochondrial proteome. Am J Physiol Cell Physiol292: C689-C697, 2006), were analyzed using a canonical metabolic pathway approach as well as a functional domain homology analysis. These data were inserted into the Kyoto Encyclopedia of Genes and Genomes pathway framework to give global and metabolic pathway-specific information on the impact of the differential protein distribution on mitochondrial function. Custom pathway analysis was also performed using pathways limited to the mitochondrion. With the use of this approach, several well-known functional differences between these mitochondrial populations were confirmed. These included GABA metabolism in the brain, urea synthesis in the liver, and the domination of oxidative phosphorylation in the heart. By comparing relative protein amounts of mitochondria across tissues, a greater understanding of functional emphasis is possible as well as the nuclear "programming" required to enhance a given function within the mitochondria. For proteins determined to be mitochondrial and lacking a defined role functional domain BLAST analyses were performed. Several proteins associated with DNA structural modification and a novel CoA transferase were identified. A protein was also identified capable of catalyzing the first three steps of de novo pyrimidine synthesis. This analysis demonstrates that the distribution of nuclear encoded proteins significantly modifies the overall functional emphasis of the mitochondria to meet tissue-specific needs. These studies demonstrate the existence of mitochondrial biochemical functions that at present are poorly defined. 10.1152/ajpcell.00109.2006}, author = {Johnson, Thor D. and Harris, Robert A. and Blair, Paul V. and Balaban, Robert S.}, citeulike-article-id = {2246744}, citeulike-linkout-0 = {http://dx.doi.org/10.1152/ajpcell.00109.2006}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16971502}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16971502}, day = {1}, doi = {10.1152/ajpcell.00109.2006}, journal = {Am J Physiol Cell Physiol}, keywords = {mitochondria, ppi, proteome, tissue}, month = {February}, number = {2}, pages = {C698--707}, posted-at = {2008-01-17 18:17:57}, priority = {3}, title = {Functional consequences of mitochondrial proteome heterogeneity}, url = {http://dx.doi.org/10.1152/ajpcell.00109.2006}, volume = {292}, year = {2007} }

TY - JOUR ID - citeulike:2246744 L3 - citeulike-article-id:2246744 N2 - Potential functional consequences of the differences in protein distribution between the mitochondria of the rat liver, heart, brain, and kidney, as determined in the companion paper in this issue (Johnson DT, French S, Blair PV, You JS, Bemis KG, Wang M, Harris RA, and Balaban RS. The tissue heterogeneity of the mammalian mitochondrial proteome. Am J Physiol Cell Physiol292: C689-C697, 2006), were analyzed using a canonical metabolic pathway approach as well as a functional domain homology analysis. These data were inserted into the Kyoto Encyclopedia of Genes and Genomes pathway framework to give global and metabolic pathway-specific information on the impact of the differential protein distribution on mitochondrial function. Custom pathway analysis was also performed using pathways limited to the mitochondrion. With the use of this approach, several well-known functional differences between these mitochondrial populations were confirmed. These included GABA metabolism in the brain, urea synthesis in the liver, and the domination of oxidative phosphorylation in the heart. By comparing relative protein amounts of mitochondria across tissues, a greater understanding of functional emphasis is possible as well as the nuclear "programming" required to enhance a given function within the mitochondria. For proteins determined to be mitochondrial and lacking a defined role functional domain BLAST analyses were performed. Several proteins associated with DNA structural modification and a novel CoA transferase were identified. A protein was also identified capable of catalyzing the first three steps of de novo pyrimidine synthesis. This analysis demonstrates that the distribution of nuclear encoded proteins significantly modifies the overall functional emphasis of the mitochondria to meet tissue-specific needs. These studies demonstrate the existence of mitochondrial biochemical functions that at present are poorly defined. 10.1152/ajpcell.00109.2006 IS - 2 JF - Am J Physiol Cell Physiol EP - 707 TI - Functional consequences of mitochondrial proteome heterogeneity VL - 292 SP - C698 KW - mitochondria KW - ppi KW - proteome KW - tissue AU - Johnson, Thor AU - Harris, Robert AU - Blair, Paul AU - Balaban, Robert PY - 2007/02/01/ UR - http://dx.doi.org/10.1152/ajpcell.00109.2006 ER -