HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Tables All Versions of this Article: 292/2/C698    most recent 00109.2006v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (17) Citing Articles via Google Scholar Google Scholar Articles by Johnson, D. T. Articles by Balaban, R. S. Search for Related Content PubMed PubMed Citation Articles by Johnson, D. T. Articles by Balaban, R. S.

SPECIAL SECTION ON MITOCHONDRIAL MODELING AND FUNCTION

Functional consequences of mitochondrial proteome heterogeneity

¹Laboratory of Cardiac Energetics, National Heart Lung and Blood Institute, National Institutes of Health, Department of Health and Human Services, Bethesda, Maryland; and ²Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana

Submitted 11 March 2006 ; accepted in final form 5 September 2006

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.

oxidative phosphorylation; liquid chromatography; mass spectrometry; electrophoresis; histone; liver; heart; kidney; brain

This article has been cited by other articles:

				D. L. Hoffman and P. S. Brookes Oxygen Sensitivity of Mitochondrial Reactive Oxygen Species Generation Depends on Metabolic Conditions J. Biol. Chem., June 12, 2009; 284(24): 16236 - 16245. [Abstract] [Full Text] [PDF]

				D. T. Johnson, R. A. Harris, S. French, A. Aponte, and R. S. Balaban Proteomic changes associated with diabetes in the BB-DP rat Am J Physiol Endocrinol Metab, March 1, 2009; 296(3): E422 - E432. [Abstract] [Full Text] [PDF]