Substrate Binding Changes Conformation of the α-, but Not the β-Subunit of Mitochondrial Processing Peptidase
Copyright policy )Substrate Binding Changes Conformation of the α-, but Not the β-Subunit of Mitochondrial Processing Peptidase
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.
- Mayo Clinic United States
- Czech Academy of Sciences Czech Republic
- Drittes Physikalisches Institut Germany
- Institute of Microbiology Switzerland
Models, Molecular, Protein Folding, Protein Conformation, Protein Renaturation, Tryptophan, Metalloendopeptidases, Saccharomyces cerevisiae, Fluorescence, Recombinant Proteins, Rats, Protein Subunits, Escherichia coli, Animals, Computer Simulation, Amino Acid Sequence, Protein Precursors, Protons, Dimerization, Synchrotrons, Protein Binding
Models, Molecular, Protein Folding, Protein Conformation, Protein Renaturation, Tryptophan, Metalloendopeptidases, Saccharomyces cerevisiae, Fluorescence, Recombinant Proteins, Rats, Protein Subunits, Escherichia coli, Animals, Computer Simulation, Amino Acid Sequence, Protein Precursors, Protons, Dimerization, Synchrotrons, Protein Binding
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