Substrate binding changes conformation of the alpha-, but not the beta-subunit of mitochondrial processing peptidase.
Arch Biochem Biophys
; 385(2): 392-6, 2001 Jan 15.
Article
em En
| MEDLINE
| ID: mdl-11368022
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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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Precursores de Proteínas
/
Saccharomyces cerevisiae
/
Metaloendopeptidases
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Arch Biochem Biophys
Ano de publicação:
2001
Tipo de documento:
Article
País de publicação:
Estados Unidos