YTA12/YMR089C Literature Guide Help

Other names published for YTA12: RCA1, m-AAA protease subunit YTA12, YMR089C

YTA12 - Function/Process (22)

ReferenceOther Genes Addressed
Augustin S, et al.  (2009) An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases. Mol Cell 35(5):574-85
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
Chen X, et al.  (2005) Enhanced mitochondrial degradation of yeast cytochrome c with amphipathic structures. Curr Genet 47(2):67-83
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
Frohlich KU  (2001) An AAA family tree. J Cell Sci 114(Pt 9):1601-2
Lemaire C, et al.  (2000) Absence of the mitochondrial AAA protease Yme1p restores F0-ATPase subunit accumulation in an oxa1 deletion mutant of Saccharomyces cerevisiae. J Biol Chem 275(31):23471-5
Leonhard K, et al.  (2000) Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface. Mol Cell 5(4):629-38
Shah ZH, et al.  (2000) The human homologue of the yeast mitochondrial AAA metalloprotease Yme1p complements a yeast yme1 disruptant. FEBS Lett 478(3):267-70
Steglich G, et al.  (1999) Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria. Mol Cell Biol 19(5):3435-42
Arlt H, et al.  (1998) The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease. EMBO J 17(16):4837-47
Beilharz T, et al.  (1998) A toxic fusion protein accumulating between the mitochondrial membranes inhibits protein assembly in vivo. J Biol Chem 273(52):35268-72
Savel'ev AS, et al.  (1998) ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system. J Biol Chem 273(32):20596-602
Swaffield JC and Purugganan MD  (1997) The evolution of the conserved ATPase domain (CAD): reconstructing the history of an ancient protein module. J Mol Evol 45(5):549-63
Arlt H, et al.  (1996) The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell 85(6):875-85
Leonhard K, et al.  (1996) AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria. EMBO J 15(16):4218-29