Suppression mechanisms of COX assembly defects in yeast and human: Insights into the COX assembly process Export

@article{citeulike:3879125, abstract = {Eukaryotic cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. COX is a multimeric enzyme formed by subunits of dual genetic origin whose assembly is intricate and highly regulated. In addition to the structural subunits, a large number of accessory factors are required to build the holoenzyme. The function of these factors is required in all stages of the assembly process. They are relevant to human health because devastating human disorders have been associated with mutations in nuclear genes encoding conserved COX assembly factors. The study of yeast strains and human cell lines from patients carrying mutations in structural subunits and COX assembly factors has been invaluable to attain the current state of knowledge, even if still fragmentary, of the COX assembly process. After the identification of the genes involved, the isolation and characterization of genetic and metabolic suppressors of COX assembly defects, reviewed here, have become a profitable strategy to gain insight into their functions and the pathways in which they operate. Additionally, they have the potential to provide useful information for devising therapeutic approaches to combat human disorders associated with COX deficiency.}, author = {Barrientos, A. and Gouget, K. and Horn, D. and Soto, I. and Fontanesi, F.}, citeulike-article-id = {3879125}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.bbamcr.2008.05.003}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0167488908001663}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/18522805}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=18522805}, doi = {10.1016/j.bbamcr.2008.05.003}, issn = {01674889}, journal = {Biochimica et Biophysica Acta (BBA) - Molecular Cell Research}, keywords = {cox2, cox3, disease, goodref, human, litrev, mitochondria, projmt, respiration, review, yeast}, month = {January}, number = {1}, pages = {97--107}, posted-at = {2009-05-07 08:52:28}, priority = {0}, title = {Suppression mechanisms of COX assembly defects in yeast and human: Insights into the COX assembly process}, url = {http://dx.doi.org/10.1016/j.bbamcr.2008.05.003}, volume = {1793}, year = {2009} }

TY - JOUR ID - citeulike:3879125 L3 - citeulike-article-id:3879125 N2 - Eukaryotic cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. COX is a multimeric enzyme formed by subunits of dual genetic origin whose assembly is intricate and highly regulated. In addition to the structural subunits, a large number of accessory factors are required to build the holoenzyme. The function of these factors is required in all stages of the assembly process. They are relevant to human health because devastating human disorders have been associated with mutations in nuclear genes encoding conserved COX assembly factors. The study of yeast strains and human cell lines from patients carrying mutations in structural subunits and COX assembly factors has been invaluable to attain the current state of knowledge, even if still fragmentary, of the COX assembly process. After the identification of the genes involved, the isolation and characterization of genetic and metabolic suppressors of COX assembly defects, reviewed here, have become a profitable strategy to gain insight into their functions and the pathways in which they operate. Additionally, they have the potential to provide useful information for devising therapeutic approaches to combat human disorders associated with COX deficiency. IS - 1 JF - Biochimica et Biophysica Acta (BBA) - Molecular Cell Research SN - 01674889 EP - 107 TI - Suppression mechanisms of COX assembly defects in yeast and human: Insights into the COX assembly process VL - 1793 SP - 97 KW - cox2 KW - cox3 KW - disease KW - goodref KW - human KW - litrev KW - mitochondria KW - projmt KW - respiration KW - review KW - yeast AU - Barrientos, A AU - Gouget, K AU - Horn, D AU - Soto, I AU - Fontanesi, F PY - 2009/01// UR - http://dx.doi.org/10.1016/j.bbamcr.2008.05.003 ER -