Covalent Attachment of FAD to the Yeast Succinate Dehydrogenase Flavoprotein Requires Import into Mitochondria, Presequence Removal, and Folding
Open Access
- 1 February 1996
- journal article
- research article
- Published by Elsevier
- Vol. 271 (8) , 4055-4060
- https://doi.org/10.1074/jbc.271.8.4055
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- A Requirement for Matrix Processing Peptidase but Not for Mitochondrial Chaperonin in the Covalent Attachment of FAD to the Yeast Succinate Dehydrogenase FlavoproteinPublished by Elsevier ,1996
- The covalent attachment of FAD to the flavoprotein of Saccharomyces cerevisiae succinate dehydrogenase is not necessary for import and assembly into mitochondriaEuropean Journal of Biochemistry, 1994
- Sorting out mitochondrial proteinsTrends in Cell Biology, 1993
- The C-terminus of the succinate dehydrogenase IP peptide of Saccharomyces cerevisiae is significant for assembly of complex IIBiochemistry, 1992
- SDH1, the gene encoding the succinate dehydrogenase flavoprotein subunit from Saccharomyces cerevisiaeGene, 1992
- Covalent cofactor binding to flavoenzymes requires specific effectorsEuropean Journal of Biochemistry, 1989
- New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sitesGene, 1988
- A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptidesNature, 1988
- Molecular biology, biochemistry and bionergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coliBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1985
- Interaction of the membrane-bound succinate dehydrogenase with substrate and competitive inhibitorsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984