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Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain.
- Source :
-
Molecular cell [Mol Cell] 1999 Mar; Vol. 3 (3), pp. 275-85. - Publication Year :
- 1999
-
Abstract
- We demonstrate that the major in vivo targets of brefeldin A (BFA) in the secretory pathway of budding yeast are the three members of the Sec7 domain family of ARF exchange factors: Gea1p and Gea2p (functionally interchangeable) and Sec7p. Specific residues within the Sec7 domain are important for BFA inhibition of ARF exchange activity, since mutations in these residues of Gea1p (sensitive to BFA) and of ARNO (resistant to BFA) reverse the sensitivity of each to BFA in vivo and in vitro. We show that the target of BFA inhibition of ARF exchange activity is an ARF-GDP-Sec7 domain protein complex, and that BFA acts to stabilize this complex to a greater extent for a BFA-sensitive Sec7 domain than for a resistant one.
- Subjects :
- ADP-Ribosylation Factors
Amino Acid Sequence
Amino Acid Substitution
Drug Resistance, Microbial
Fungal Proteins chemistry
Fungal Proteins genetics
Fungal Proteins isolation & purification
GTP-Binding Proteins chemistry
GTP-Binding Proteins genetics
GTP-Binding Proteins isolation & purification
Gene Dosage
Guanosine Triphosphate metabolism
Kinetics
Molecular Sequence Data
Mutation
Recombinant Fusion Proteins biosynthesis
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins isolation & purification
Recombinant Fusion Proteins metabolism
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae growth & development
Saccharomyces cerevisiae metabolism
Antifungal Agents pharmacology
Brefeldin A pharmacology
Fungal Proteins metabolism
GTP-Binding Proteins metabolism
GTPase-Activating Proteins
Guanine Nucleotide Exchange Factors
Guanosine Diphosphate metabolism
Saccharomyces cerevisiae drug effects
Saccharomyces cerevisiae Proteins
Subjects
Details
- Language :
- English
- ISSN :
- 1097-2765
- Volume :
- 3
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 10198630
- Full Text :
- https://doi.org/10.1016/s1097-2765(00)80455-4