AFG3/YER017C Literature Guide Help

Other names published for AFG3: YTA10, AAA family ATPase AFG3, YER017C

AFG3 - Mutants/Phenotypes (45)

ReferenceOther Genes Addressed
Delaney JR, et al.  (2013) Stress profiling of longevity mutants identifies Afg3 as a mitochondrial determinant of cytoplasmic mRNA translation and aging. Aging Cell 12(1):156-66
Khalimonchuk O, et al.  (2012) Selective Oma1 protease-mediated proteolysis of Cox1 subunit of cytochrome oxidase in assembly mutants. J Biol Chem 287(10):7289-300
Barreto L, et al.  (2011) A genomewide screen for tolerance to cationic drugs reveals genes important for potassium homeostasis in Saccharomyces cerevisiae. Eukaryot Cell 10(9):1241-50
Bonn F, et al.  (2011) Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria. EMBO J 30(13):2545-56
Delaney JR, et al.  (2011) Quantitative evidence for early life fitness defects from 32 longevity-associated alleles in yeast. Cell Cycle 10(1):156-65
Delaney JR, et al.  (2011) Sir2 deletion prevents lifespan extension in 32 long-lived mutants. Aging Cell 10(6):1089-91
Francis BR and Thorsness PE  (2011) Hsp90 and mitochondrial proteases Yme1 and Yta10/12 participate in ATP synthase assembly in Saccharomyces cerevisiae. Mitochondrion 11(4):587-600
Kaur J and Stuart RA  (2011) Truncation of the Mrp20 protein reveals new ribosome-assembly subcomplex in mitochondria.LID - 10.1038/embor.2011.133 [doi] EMBO Rep ()
Pierson TM, et al.  (2011) Whole-Exome Sequencing Identifies Homozygous AFG3L2 Mutations in a Spastic Ataxia-Neuropathy Syndrome Linked to Mitochondrial m-AAA Proteases. PLoS Genet 7(10):e1002325
Cooper SJ, et al.  (2010) High-throughput profiling of amino acids in strains of the Saccharomyces cerevisiae deletion collection. Genome Res 20(9):1288-96
Augustin S, et al.  (2009) An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell 35(5):574-85
Osman C, et al.  (2009) The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria. J Cell Biol 184(4):583-96
Suppanz IE, et al.  (2009) The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol Biol Cell 20(2):572-80
Westmoreland TJ, et al.  (2009) Comparative genome-wide screening identifies a conserved doxorubicin repair network that is diploid specific in Saccharomyces cerevisiae. PLoS ONE 4(6):e5830
Shima J, et al.  (2008) Possible roles of vacuolar H(+)-ATPase and mitochondrial function in tolerance to air-drying stress revealed by genome-wide screening of Saccharomyces cerevisiae deletion strains. Yeast 25(3):179-90
Smith ED, et al.  (2008) Quantitative evidence for conserved longevity pathways between divergent eukaryotic species. Genome Res 18(4):564-70
Duvezin-Caubet S, et al.  (2007) OPA1 Processing Reconstituted in Yeast Depends on the Subunit Composition of the m-AAA Protease in Mitochondria. Mol Biol Cell 18(9):3582-3590
Tatsuta T, et al.  (2007) m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria. EMBO J 26(2):325-35
Xia L, et al.  (2007) Identification of genes required for protection from doxorubicin by a genome-wide screen in Saccharomyces cerevisiae. Cancer Res 67(23):11411-8
Ishihara N, et al.  (2006) Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J 25(13):2966-77
Chen X, et al.  (2005) Enhanced mitochondrial degradation of yeast cytochrome c with amphipathic structures. Curr Genet 47(2):67-83
Michaelis G, et al.  (2005) Mitochondrial signal peptidases of yeast: the rhomboid peptidase Pcp1 and its substrate cytochrome C peroxidase. Gene 354():58-63
Nolden M, et al.  (2005) The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123(2):277-89
Jonson L, et al.  (2004) Enhanced peptide secretion by gene disruption of CYM1, a novel protease in Saccharomyces cerevisiae. Eur J Biochem 271(23-24):4788-97
Korbel D, et al.  (2004) Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits. EMBO Rep 5(7):698-703
Atorino L, et al.  (2003) Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J Cell Biol 163(4):777-87
Kaser M, et al.  (2003) Oma1, a novel membrane-bound metallopeptidase in mitochondria with activities overlapping with the m-AAA protease. J Biol Chem 278(47):46414-23
Dimmer KS, et al.  (2002) Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell 13(3):847-53
Esser K, et al.  (2002) A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1. J Mol Biol 323(5):835-43
Broadley SA, et al.  (2001) Peripheral mitochondrial inner membrane protein, Mss2p, required for export of the mitochondrially coded Cox2p C tail in Saccharomyces cerevisiae. Mol Cell Biol 21(22):7663-72