AFG3/YER017C Literature Guide Help

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

AFG3 - Cellular Location (20)

ReferenceOther Genes Addressed
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
Reinders J, et al.  (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5(7):1543-54
Meier S, et al.  (2005) Proline residues of transmembrane domains determine the sorting of inner membrane proteins in mitochondria. J Cell Biol 170(6):881-8
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
Sickmann A, et al.  (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100(23):13207-12
Baumann F, et al.  (2002) Insertion of bitopic membrane proteins into the inner membrane of mitochondria involves an export step from the matrix. J Biol Chem 277(24):21405-13
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
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
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
Guzelin E, et al.  (1996) Afg3p, a mitochondrial ATP-dependent metalloprotease, is involved in degradation of mitochondrially-encoded Cox1, Cox3, Cob, Su6, Su8 and Su9 subunits of the inner membrane complexes III, IV and V. FEBS Lett 381(1-2):42-6
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
Rep M, et al.  (1996) Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon. Science 274(5284):103-6
Rep M, et al.  (1996) Three genes for mitochondrial proteins suppress null-mutations in both Afg3 and Rca1 when over-expressed. Curr Genet 30(3):206-11
Paul MF and Tzagoloff A  (1995) Mutations in RCA1 and AFG3 inhibit F1-ATPase assembly in Saccharomyces cerevisiae. FEBS Lett 373(1):66-70
Guelin E, et al.  (1994) Sequence of the AFG3 gene encoding a new member of the FtsH/Yme1/Tma subfamily of the AAA-protein family. Yeast 10(10):1389-94
Pajic A, et al.  (1994) Yta10p is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria. FEBS Lett 353(2):201-6
Tauer R, et al.  (1994) Yta10p, a member of a novel ATPase family in yeast, is essential for mitochondrial function. FEBS Lett 353(2):197-200