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Information on EC 3.4.24.B18 - m-AAA protease and Organism(s) Saccharomyces cerevisiae and UniProt Accession P40341
for references in articles please use BRENDA:EC3.4.24.B18preliminary BRENDA-supplied EC number
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3.4.24.B18 m-AAA proteaseSpecify your search results
Word Map
- 3.4.24.B18
- paraplegia
- hereditary
- ataxia
- spinocerebellar
- atpases
- oma1
-
proteostasis
-
cristae
-
dynamin-like
-
homo-oligomeric
- paraparesis
- spastin
-
hetero-oligomeric
-
inner-membrane
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
afg3l2, paraplegin, yme1l, m-aaa protease, afg3l1, aaa protease, yta10, yta12, yta12p, mitochondrial aaa protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
mitochondrial respiratory chain complexes assembly protein RCA1
-
Yta10
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
conserved metal-binding site HEXXH, selective degradation, mechanism
-
proteolytic degradation of proteins
degradation of hydrophobic membrane-spanning segments of misfolded mitochondrial membrane proteins
-
proteolytic degradation of proteins
enzyme shows overlapping substrate specificity with the ATP-dependent PIM1 protease located in the mitochondrial matrix
-
proteolytic degradation of proteins
m-AAA protease shows overlapping substrate specificity with the i-AAA protease, enzyme degrades domains of substrate proteins exposed to the opposite membrane surface, active site contains the conserved motif HEXXH, a helical region is located at the extreme C-terminus of the subunit
-
proteolytic degradation of proteins
mechanism, m-AAA protease shows overlapping substrate specificity with the i-AAA protease, intermolecular catalytic role of SRH domain at the C-terminus of the AAA domain, m-AAA protease shows overlapping substrate specificity with the i-AAA protease, enzyme degrades domains of substrate proteins exposed to the opposite membrane surface, active site contains the conserved motif HEXXH, a helical region is located at the extreme C-terminus of the subunit
-
proteolytic degradation of proteins
overlapping substrate specificity with i-AAA protease EC 3.4.24.B19, mechanism, reaction involves an active extraction of transmembrane segments and transport of solvent-exposed domains across the membrane, inner membrane proteins, active site at the opposite membrane surface
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
213390-44-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
apocytochrome P450scc + H2O
?
-
bovine protein substrate from adrenal cortex mitochondrial inner membrane, imported in vitro into isolated yeast mitochondrial membrane, due to an N-terminal fusion to a heterologous transmembrane region
-
?
Ccp1 precursor + H2O
?
-
i.e. cytochrome c peroxidase, natural substrate
-
-
?
hybrid protein + H2O
2 peptide fragments f2 and f3
-
hybrid protein of subunit 2 of cytochrome oxidase residues 1-74, mouse dihydrofolate reductase, and mitochondrial presequence, residues 1-66, of subunit 9 of the ATPase of Neurospora crassa, in vitro import into the mitochondrion
product characterization
?
mitochondrial integral inner membrane protein Mgm1 + H2O
?
-
-
-
-
?
mitochondrial integral inner membrane protein Yme2p + H2O
?
-
wild-type and chimeric mutant containing the dihydrofolate reductase loosely folded mutant, not the one containing the wild-type dihydrofolate reductase, overview, unfolding of the substrate at one side of the membrane might be sufficient for proteolysis, in vitro synthesized protein substrate, imported into the mitochondria, spans the membrane once and exposes large domains at both membrane surfaces
-
?
protein Atp7 + H2O
?
-
subunit of F1Fo-ATP synthase, peripheral membrane protein
-
-
?
protein Cob + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein Cox1 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein Cox3 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein F0 subunit 6 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein F0 subunit 8 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein F0 subunit 9 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
residues 1-74 of subunit 2 of cytochrome oxidase + H2O
?
-
two-step procedure, in vitro import into the mitochondrion
-
?
cytochrome c peroxidase + H2O
?
-
the m-AAA protease is enriched in the inner boundary membrane of mitochondria. The membrane-anchored precursor form of cytochrome c peroxidase (pCcp1) is preferentially localized in this subdomain of the inner membrane. On processing by the m-AAA protease and rhomboid protease Pcp1, the mature Ccp1 is released and moves into the cristae space
-
-
?
cytochrome c peroxidase 1 + H2O
?
-
mediates the ATP-dependent membrane dislocation of cytochrome c peroxidase 1 independent of its proteolytic activity, it thereby ensures the correct positioning of cytochrome c peroxidase 1 within the membrane bilayer allowing intramembrane cleavage by rhomboid
-
-
?
cytochrome c peroxidase 1 + H2O
?
-
cleaved at Ala29 in the middle of the hydrophobic segment by the inner membrane m-AAA protease complex
-
-
?
MrpL32 + H2O
?
-
mitochondrial ribosomal protein, enzyme mediates processing of newly imported MrpL32. Maturation in vivo depends on enzyme
-
-
?
MrpL32 + H2O
?
-
mitochondrial ribosomal protein, enzyme mediates processing of newly imported MrpL32
-
-
?
MrpL32 + H2O
?
-
in vivo substrate, m-AAA does not affect the stability of the protein but cleaves the N-terminal mitochondrial targeting sequence upon protein import into the mitochondrion
-
-
?
MrpL32 + H2O
?
-
m-AAA protease initiates proteolysis from the N-terminus of MrpL32. Oxidative stress impairs folding of MrpL32, resulting in its degradation by the m-AAA protease
-
-
?
MrpL32 + H2O
?
-
MrpL32 receives processing by the m-AAA protease after import into the matrix
-
-
?
protein + H2O
peptides
-
activity depends on oligomerisation
-
?
protein + H2O
peptides
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
product peptides in the matrix space are actively transported across the inner membrane by an ABC transporter Mdl1
?
protein + H2O
peptides
-
degradation of proteins exposing loops or domain at either sides of the mitochondrial inner membrane
-
?
protein + H2O
peptides
-
enzyme probably forms a pore-like structure facilitating the transport of hydrophilic parts of the substrate protein during its extraction, limited substrate recognition
product peptides in the matrix space are actively transported across the inner membrane by an ABC transporter Mdl1
?
protein + H2O
peptides
-
degradation of mislocalized proteins in the mitochodria
-
?
protein + H2O
peptides
-
enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans
-
?
protein + H2O
peptides
-
important role in the removal of non-assembled polypeptides from the inner membrane, inactivation of the enzyme is lethal, loss of activity causes respiration-deficiency, affects the splicing of transcripts of mitochondrial genes encoding essential respiratory chain subunits and controls the post-translational asembly of respiratory complexes and the ATP synthase, required as a membrane-integrated quality control to facilitate protein folding and to ensure the selective removal of non-native polypeptides
-
?
protein + H2O
peptides
-
quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability
-
?
additional information
?
-
-
construction of several deletion mutants of Yme2p and investigation of their behaviour as substrates, overview, the folded intermembrane space domain of Yme2p prevents proteolysis but not protease binding at the opposite membrane side
-
?
additional information
?
-
-
Yta12p enzyme requires YTA10-12 complex formation for activity
-
?
additional information
?
-
-
m-AAA protease ensures maturation of cytochrome c peroxidase 1 (Ccp1). The precursor of Ccp1 is dislocated from the inner mitochondrial membrane to allow cleavage by the rhomboid protease Pcp1. Dislocation depends on the ATPase but not the proteolytic activity of the m-AAA protease
-
-
?
additional information
?
-
-
Mgm1 is not a substrate of the enzyme
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ccp1 precursor + H2O
?
-
i.e. cytochrome c peroxidase, natural substrate
-
-
?
cytochrome c peroxidase + H2O
?
-
the m-AAA protease is enriched in the inner boundary membrane of mitochondria. The membrane-anchored precursor form of cytochrome c peroxidase (pCcp1) is preferentially localized in this subdomain of the inner membrane. On processing by the m-AAA protease and rhomboid protease Pcp1, the mature Ccp1 is released and moves into the cristae space
-
-
?
cytochrome c peroxidase 1 + H2O
?
-
cleaved at Ala29 in the middle of the hydrophobic segment by the inner membrane m-AAA protease complex
-
-
?
protein Atp7 + H2O
?
-
subunit of F1Fo-ATP synthase, peripheral membrane protein
-
-
?
protein Cob + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein Cox1 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein Cox3 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein F0 subunit 6 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein F0 subunit 8 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein F0 subunit 9 + H2O
?
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
MrpL32 + H2O
?
-
mitochondrial ribosomal protein, enzyme mediates processing of newly imported MrpL32. Maturation in vivo depends on enzyme
-
-
?
MrpL32 + H2O
?
-
in vivo substrate, m-AAA does not affect the stability of the protein but cleaves the N-terminal mitochondrial targeting sequence upon protein import into the mitochondrion
-
-
?
MrpL32 + H2O
?
-
m-AAA protease initiates proteolysis from the N-terminus of MrpL32. Oxidative stress impairs folding of MrpL32, resulting in its degradation by the m-AAA protease
-
-
?
MrpL32 + H2O
?
-
MrpL32 receives processing by the m-AAA protease after import into the matrix
-
-
?
protein + H2O
peptides
-
degradation of proteins exposing loops or domain at either sides of the mitochondrial inner membrane
-
?
protein + H2O
peptides
-
degradation of mislocalized proteins in the mitochodria
-
?
protein + H2O
peptides
-
enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans
-
?
protein + H2O
peptides
-
important role in the removal of non-assembled polypeptides from the inner membrane, inactivation of the enzyme is lethal, loss of activity causes respiration-deficiency, affects the splicing of transcripts of mitochondrial genes encoding essential respiratory chain subunits and controls the post-translational asembly of respiratory complexes and the ATP synthase, required as a membrane-integrated quality control to facilitate protein folding and to ensure the selective removal of non-native polypeptides
-
?
protein + H2O
peptides
-
quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability
-
?
additional information
?
-
-
m-AAA protease ensures maturation of cytochrome c peroxidase 1 (Ccp1). The precursor of Ccp1 is dislocated from the inner mitochondrial membrane to allow cleavage by the rhomboid protease Pcp1. Dislocation depends on the ATPase but not the proteolytic activity of the m-AAA protease
-
-
?
additional information
?
-
-
Mgm1 is not a substrate of the enzyme
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
ATP binding is required for enzyme assembly, enzyme contains conserved Walker-type ATPase domain of approximately 230 amino acids, dependent on
ATP
-
dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family
ATP
-
dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family, hydrolysis induces conformational changes of the AAA domain driving substrate unfolding and dislocation from the membrane
ATP
-
intersubunit coordination of the ATP hydrolysis leads to an ordered ATP hydrolysis within the AAA ring, which ensures efficient substrate dislocation from the membrane and translocation to the proteolytic chamber
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a consensus metal-binding site represents the proteolytic centre, metallopeptidase of the M41 family
additional information
-
conserved metal-binding motif HEXGH at the proteolytic centre
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
prohibitin
-
located at the periphery of mitochondria at protein import sites, has a regulatory role, deletion of prohibitin leads to accelerated degradation of non-assembled membrane proteins by the m-AAA protease, overexpression of prohibitin stabilizes non-native polypeptides against degradation
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no activity at 25°C, unfolding of Yme2p at 37°C triggers its proteolytic breakdown
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
both subunit types span the membrane twice, integral, active at the matrix side of the inner membrane
-
inner side, exposes catalytic sites to the mitochondrial matrix
-
integral, active at the matrix side of the inner membrane
-
the m-AAA protease is a conserved hetero-oligomeric complex in the inner membrane of mitochondria. m-AAA protease is preferentially localized in the inner boundary membrane compared to the cristae membrane
-
-
-
active on the matrix side of the inner membrane
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the m-AAA protease dislocates transmembrane segments from the mitochondrial inner membrane. The presence of the m-AAA protease increases the hydrophobicity required for a transmembrane segment to remain in the membrane. The m-AAA protease is a central component of the mitochondrial protein quality control system, being able to extract and degrade misfolded polypeptides from the inner membrane
physiological function
physiological function
-
MrpL32 ribosomal subunit processing is the central process controlled by the m-AAA protease in yeast
physiological function
in a mechanistic model, the ATP-bound subunits bind substrate, whereas the ADP-bound subunit releases the substrate at the lowest position of the spiral staircase, and the nucleotide-free subunit transitions to the highest position of the spiral staircase, where it reattaches to the substrate upon ATP-binding. The unfolded substrate is translocated in this fashion toward the negatively charged proteolytic chamber, where it is positioned for cleavage at the zinc-coordinated active site of the immutable planar protease domains
physiological function
-
replacement of the subunit Yta10 TM2 domain abolishes membrane dislocation for only a subset of substrates, whereas replacement of the subunit Yta12 TM2 domain impairs membrane dislocation for all substrates tested. m-AAA protease-mediated membrane dislocation is impaired in the presence of a large downstream hydrophilic moiety in a membrane substrate
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme is part of a supercomplex in the inner mitochondrial membrane with a native MW of approximately 2000 kDa, assembling with the prohibitin complex
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
additional information
oligomer
-
homooligomeric, subunits Yta10p and Yta12p, i.e. Afg3p and Rca1p
additional information
-
formation of a supercomplex between the enzyme and a large complex containing the prohibitin homologues Phb1p and Phb2p, ATP binding is required for enzyme assembly
additional information
-
subunits span the membrane twice, activity depends on oligomerisation, the enzyme consists of a AAA domain, providing chaperone-like properties and binding to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic domain, and a Walker-type P-loop ATPase domain
additional information
-
the enzyme consists of an AAA domain, providing chaperone-like properties and binding to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic doamin, and a Walker-type P-loop ATPase domain, both subunits span the membrane twice
additional information
-
interaction of enzyme with prohibitin proteins Phb1 and Phb2 of the inner mitochondrial membrane
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3.4 A cryo-EM structure. The ATPase domains engage substrates through a double spiral staircase of tyrosines. The enzyme contains three co-existing nucleotide states, and the spiral staircase organization links nucleotide state to pore loop conformation. A hinge-like glycine linker accommodates ATPase rearrangements above a flat protease ring
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E388Q/E448Q
-
an ATP hydrolysis-deficient m-AAA protease variant. The mutant effectively traps ATP and keeps m-AAA protease subunits in one nucleotide conformation
E559Q
E614Q
additional information
E559Q
-
of subunit Yta10, enzyme is still capable of substrate binding but lacks proteolytic activity
E614Q
-
site-directed mutagenesis, exchange of active site residue, stongly reduced activity
E614Q
-
of subunit Yta12, enzyme is still capable of substrate binding but lacks proteolytic activity
additional information
-
construction of chimeric protein substrates: 1. the matrix domain of Yme2p is replaced by mouse dihydrofolate reductase, 2. a chimeric protein consisting of a loosely folded mutant variant of dihydrofolate reductase and the C-terminal end of Yme2p
additional information
-
inactivation of the enzyme impairs respiratory competence
additional information
-
deletion of either subunit Yta10 or Yta12, partial stabilization of substrate Atp7. Deletion of transmembrane segments of either subunit Yta10 or Yta12, enzyme retains proteolytic activity, but proteolsis of integral membrane proteins is impaired. Transmembrane segments of enzyme have a direct role in the dislocation of membrane-embedded subsrates
additional information
-
deletion of either subunit Yta10 or Yta12, synthesis of mitochondrially encoded proteins is strongly impaired
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography and Superose 6 gel filtration
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Saccharomyces cerevisiae (P40341)
Langer, T.; Kaser, M.; Klanner, C.; Leonhard, K.
AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis
Biochem. Soc. Trans.
29
431-436
2001
eukaryota, Saccharomyces cerevisiae
Arnold, I.; Langer, T.
Membrane protein degradation by AAA proteases in mitochondria
Biochim. Biophys. Acta
1592
89-96
2002
Saccharomyces cerevisiae
Leonhard, K.; Herrmann, J.M.; Stuart, R.A.; Mannhaupt, G.; Neupert, W.; Langer, T.
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
4218-4229
1996
Saccharomyces cerevisiae
Savel'ev, A.S.; Novikova, L.A.; Kovaleva, I.E.; Luzikov, V.N.; Neupert, W.; Langer, T.
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
20596-20602
1998
Saccharomyces cerevisiae
Leonhard, K.; Guiard, B.; Pellecchia, G.; Tzagoloff, A.; Neupert, W.; Langer, T.
Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface
Mol. Cell
5
629-638
2000
Saccharomyces cerevisiae
Nolden, M.; Ehses, S.; Koppen, M.; Bernacchia, A.; Rugarli, E.I.; Langer, T.
The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria
Cell
123
277-289
2005
Saccharomyces cerevisiae, Mus musculus
Korbel, D.; Wurth, S.; Kaeser, M.; Langer, T.
Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits
EMBO Rep.
5
698-703
2004
Saccharomyces cerevisiae
Tatsuta, T.; Augustin, S.; Nolden, M.; Friedrichs, B.; Langer, T.
m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria
EMBO J.
26
325-335
2007
Saccharomyces cerevisiae
Rugarli, E.I.; Langer, T.
Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia
Trends Mol. Med.
12
262-269
2006
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
Suppanz, I.E.; Wurm, C.A.; Wenzel, D.; Jakobs, S.
The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria
Mol. Biol. Cell
20
572-580
2009
Saccharomyces cerevisiae
Gerdes, F.; Tatsuta, T.; Langer, T.
Mitochondrial AAA proteases - Towards a molecular understanding of membrane-bound proteolytic machines
Biochim. Biophys. Acta
1823
49-55
2012
Saccharomyces cerevisiae
Bonn, F.; Tatsuta, T.; Petrungaro, C.; Riemer, J.; Langer, T.
Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria
EMBO J.
30
2545-2556
2011
Saccharomyces cerevisiae
Lee, S.; Augustin, S.; Tatsuta, T.; Gerdes, F.; Langer, T.; Tsai, F.T.
Electron cryomicroscopy structure of a membrane-anchored mitochondrial AAA protease
J. Biol. Chem.
286
4404-4411
2011
Saccharomyces cerevisiae
Botelho, S.C.; Tatsuta, T.; von Heijne, G.; Kim, H.
Dislocation by the m-AAA protease increases the threshold hydrophobicity for retention of transmembrane helices in the inner membrane of yeast mitochondria
J. Biol. Chem.
288
4792-4798
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
Lee, S.; Lee, H.; Yoo, S.; Kim, H.
Molecular insights into the m-AAA protease-mediated dislocation of transmembrane helices in the mitochondrial inner membrane
J. Biol. Chem.
292
20058-20066
2017
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
Puchades, C.; Rampello, A.; Shin, M.; Giuliano, C.; Wiseman, R.; Glynn, S.; Lander, G.
Atomic structure of the mitochondrial inner membrane AAA+ protease YME1 reveals the mecanism of substrate processing
Science
358
6363
2017
Saccharomyces cerevisiae (B3LL85), Saccharomyces cerevisiae RM11-1a (B3LL85)
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