The C-terminus of the succinate dehydrogenase IP peptide of Saccharomyces cerevisiae is significant for assembly of complex II.
Biochemistry
; 31(36): 8442-8, 1992 Sep 15.
Article
em En
| MEDLINE
| ID: mdl-1390628
ABSTRACT
Site-directed mutagenesis was used to introduce mutations into the gene for the iron protein (IP) of succinate dehydrogenase (SDH) of Saccharomyces cerevisiae. Specifically, three mutations were examined which caused the synthesis of truncated IP peptides missing four, seven, or 17 amino acids from the C-terminus, respectively. The deletion of seven or more amino acids includes the loss of two lysine residues, which appear to have been highly conserved in evolution. While the deletion of four amino acids had no effect on the assembly of complex II and on its activity, the deletion including the two lysines abolished SDS activity completely and led to the failure of the imported IP peptide to be incorporated into a stable complex II or SDH complex. Replacement of one of the lysines by threonine had no effect, but replacement of both by threonine affected the specific activity of complex II but not its assembly and stability.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
/
Succinato Desidrogenase
/
Metaloproteínas
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
1992
Tipo de documento:
Article