Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria

EMBO Journal

Volumn 30, Issue 13, 2011, Pages 2545-2556

  Bonn, Florian ^a   Tatsuta, Takashi ^a   Petrungaro, Carmelina ^b   Riemer, Jan ^b   Langer, Thomas ^a,c  

^a UNIVERSITY OF COLOGNE   (Germany)

^b Rheinland Pfälzische Technische Universität Kaiserslautern Landau   (Germany)

^c MAX PLANCK INSTITUTE FOR BIOLOGY OF AGEING   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

M AAA PROTEASE; POLYPEPTIDE; PROTEIN MRPL32; PROTEIN SECA; PROTEIN SUBUNIT; PROTEINASE; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BIOGENESIS; DEGENERATIVE DISEASE; ENZYME ACTIVITY; MITOCHONDRIAL MEMBRANE; NERVE CELL NECROSIS; NONHUMAN; PRESEQUENCE ASSISTED FOLDING; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN PROCESSING; RIBOSOME SUBUNIT; YEAST CELL;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; DEINOCOCCUS; METALLOENDOPEPTIDASES; MITOCHONDRIA; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; ORGANISMS, GENETICALLY MODIFIED; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN TRANSPORT; RIBOSOMAL PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ANALYSIS, PROTEIN; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 79960047807     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2011.169     Document Type: Article

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