Substrate evokes translocation of both domains in the mitochondrial processing peptidase α-subunit during which the C-terminus acts as a stabilizing element

Biochemical and Biophysical Research Communications

Volumn 316, Issue 1, 2004, Pages 211-217

  Janata, Jiří ^a   Holá, Klára ^a   Kubala, Martin ^b,c   Gakh, Oleksandr ^d   Parkhomenko, Natalya ^a   Matušková, Anna ^a   Kutejová, Eva ^e   Amler, Evžen ^b,c  

^a INSTITUTE OF MICROBIOLOGY   (Czech Republic)

^b INSTITUTE OF PHYSIOLOGY   (Czech Republic)

^c CHARLES UNIVERSITY   (Czech Republic)

^d MAYO CLINIC   (United States)

^e INSTITUTE OF CHEMISTRY   (Slovakia)

Author keywords

Metallopeptidase; Mitochondria; Mitochondrial processing peptidase; Presequence; Processing; Substrate recognition; Tryptophan fluorescence measurement

Indexed keywords

AMINO ACID; MITOCHONDRIAL ENZYME; PEPTIDASE; PROTEIN SUBUNIT; STABILIZING AGENT; TRYPTOPHAN;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; FLUORESCENCE; GENE DELETION; GENE MUTATION; MITOCHONDRION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION;

AMINO ACID SUBSTITUTION; FUNGAL PROTEINS; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN PRECURSORS; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PROTEIN TRANSPORT; SEQUENCE DELETION; TRYPTOPHAN;

EID: 1542285493     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.02.025     Document Type: Article

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