Substrate binding changes conformation of the alpha-, but not the beta-subunit of mitochondrial processing peptidase
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
11368022
DOI
10.1006/abbi.2000.2167
PII: S0003-9861(00)92167-2
Knihovny.cz E-resources
- MeSH
- Dimerization MeSH
- Escherichia coli genetics MeSH
- Fluorescence MeSH
- Protein Conformation MeSH
- Rats MeSH
- Metalloendopeptidases chemistry genetics metabolism MeSH
- Models, Molecular MeSH
- Mitochondrial Processing Peptidase MeSH
- Computer Simulation MeSH
- Protein Subunits MeSH
- Protein Precursors metabolism MeSH
- Protons MeSH
- Recombinant Proteins chemistry metabolism MeSH
- Protein Renaturation MeSH
- Saccharomyces cerevisiae enzymology genetics MeSH
- Protein Folding MeSH
- Amino Acid Sequence MeSH
- Synchrotrons MeSH
- Two-Hybrid System Techniques MeSH
- Tryptophan metabolism MeSH
- Protein Binding MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Metalloendopeptidases MeSH
- Protein Subunits MeSH
- Protein Precursors MeSH
- Protons MeSH
- Recombinant Proteins MeSH
- Tryptophan MeSH
Lifetime analysis of tryptophan fluorescence of the mitochondrial processing peptidase (MPP) from Saccharomyces cerevisiae clearly proved that substrate binding evoked a conformational change of the alpha-subunit while presence of substrate influenced neither the lifetime components nor the average lifetime of the tryptophan excited state of the beta-MPP subunit. Interestingly, lifetime analysis of tryptophan fluorescence decay of the alpha-MPP subunit revealed about 11% of steady-state fractional intensity due to the long-lived lifetime component, indicating that at least one tryptophan residue is partly buried at the hydrophobic microenvironment. Computer modeling, however, predicted none of three tryptophans, which the alpha-subunit contains, as deeply buried in the protein matrix. We conclude this as a consequence of a possible dimeric (oligomeric) structure.
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