Mutations within the first LSGGQ motif of Ste6p cause defects in a-factor transport and mating in Saccharomyces cerevisiae
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Summary
It appears that several missense mutations introduced in or near the conserved LSGGQ motif within the first nucleotide-binding domain of Ste6p interfere with the ability of Ste 6p to transport a-factor out of the MATa cell.
- Type
- article
- Published
- 1996-03-01
- Cited by
- 33
- References
- 54
- Access
- Open access
- OpenAlex
- https://openalex.org/W1962293554
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:40256302
Keywords
Biology, Saccharomyces cerevisiae, ATP-binding cassette transporter, Mating of yeast, Genetics
References
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- Methods in Yeast Genetics: A Laboratory Course Manual
- Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans.
- A short course in bacterial genetics
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- One-step gene disruption in yeast.
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- Substitutions in the hydrophobic core of the alpha-factor receptor of Saccharomyces cerevisiae permit response to Saccharomyces kluyveri alpha-factor and to antagonist
- Negative regulation of STE6 gene expression by the alpha 2 product of Saccharomyces cerevisiae
- Courtship in Saccharomyces cerevisiae: an early cell-cell interaction during mating
- Molecular determinants of bioactivity of the Saccharomyces cerevisiae lipopeptide mating pheromone.
- Different structure-function relationships for alpha-factor-induced morphogenesis and agglutination in Saccharomyces cerevisiae
- New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites.
- Transformation of intact yeast cells treated with alkali cations.
- Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis.
Cited by
- Unusual Secretory Pathways: From Bacteria to Man
- Functional assays for analysis of yeast ste6 mutants.
- Fungal ABC proteins: pleiotropic drug resistance, stress response and cellular detoxification.
- Functionally Relevant Residues of Cdr1p: A Multidrug ABC Transporter of Human Pathogenic Candida albicans
- Mutations at the Signature Sequence of CFTR Create a Cd2+-gated Chloride Channel
- Endosomal transport function in yeast requires a novel AAA‐type ATPase, Vps4p
- Mutations in the Yeast Hsp40 Chaperone Protein Ydj1 Cause Defects in Axl1 Biogenesis and Pro-a-factor Processing*
- Synergy between Conserved ABC Signature Ser Residues in P-glycoprotein Catalysis*
- Inventory and function of yeast ABC proteins: about sex, stress, pleiotropic drug and heavy metal resistance.
- Mutations in the white gene of Drosophila melanogaster affecting ABC transporters that determine eye colouration.
- A novel SMC protein complex in Schizosaccharomyces pombe contains the Rad18 DNA repair protein
- Divergent Signature motifs of Nucleotide Binding Domains of ABC multidrug transporter, CaCdr1p of pathogenic Candida albicans, are functionally asymmetric and non interchangeable
- Function of prokaryotic and eukaryotic ABC proteins in lipid transport.
- The ABC‐transporter signature motif is required for peptide translocation but not peptide binding by TAP
- Functional consequences of mutations in the conserved 'signature sequence' of the ATP-binding-cassette protein MalK.
- Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile
- ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains.
- The ABCs of immunology: structure and function of TAP, the transporter associated with antigen processing.
- Functional Residues in Proteins
- Phosphoinositide signaling and turnover: PtdIns(3)P, a regulator of membrane traffic, is transported to the vacuole and degraded by a process that requires lumenal vacuolar hydrolase activities
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