Disease relevance of CTP1

• The gene encoding the mitochondrial citrate transport protein (CTP) in the yeast Saccharomyces cerevisiae has been identified, and its protein product has been overexpressed in Escherichia coli [1].

High impact information on CTP1

• Utilizing site-directed mutagenesis in combination with chemical modification of mutated residues, we have studied the roles of cysteine and arginine residues in the mitochondrial citrate transport protein (CTP) from Saccharomyces cerevisiae [2].
• The yeast mitochondrial citrate transport protein. Probing the secondary structure of transmembrane domain iv and identification of residues that likely comprise a portion of the citrate translocation pathway [3].
• In contrast, mutations in peroxisomal citrate synthase (CS2-) or in other tricarboxylic acid cycle enzymes did not result in changes in mitochondrial citrate transport, suggesting a specific functional role for mitochondrial citrate synthase in citrate transport [4].
• To explore the spatial organization and functional dynamics of the citrate transport protein (CTP), a nitroxide scan was carried out along 22 consecutive residues within the fourth transmembrane domain (TMDIV) [5].
• Utilizing cysteine scanning mutagenesis, with functional Cys-less citrate transport protein (CTP) serving as the starting template, we previously demonstrated that four single-Cys mutants located in transmembrane domains III and IV, rendered the CTP nonfunctional [6].

Biological context of CTP1

• The nuclear gene encoding the mitochondrial citrate transport protein (i.e., CTP1) has been deleted from a haploid yeast strain [7].
• Deletion of CTP1 did not lead to a phenotype on any carbon source tested, indicating that CTP1 is not an essential gene [7].
• The putative gene product of ORF YBR2039 was homologous to the group of uncoupling proteins involved in the mitochondrial energy transfer system [8].

Associations of CTP1 with chemical compounds

• The mitochondrial citrate transport protein (CTP) has been investigated by replacing 22 consecutive residues within transmembrane domain IV, one at a time, with cysteine [3].
• Ca(2+)- and citrate transport were found to be maximal at this growth phase [9].
• The mitochondrial citrate transport protein: Evidence for a steric interaction between glutamine 182 and leucine 120 and its relationship to the substrate translocation pathway and identification of other mechanistically essential residues [10].
• Previous examination of the accessibility of a panel of single-Cys mutants in transmembrane domain III (TMDIII) of the yeast mitochondrial citrate transport protein to the hydrophilic, cysteine-specific methanethiosulfonate reagent MTSES enabled identification of the water-accessible surface of this TMD [10].

Other interactions of CTP1

• The stable yeast deletion strain was constructed by homologous recombination of the HIS3 gene at the CTP1 gene locus [7].

Analytical, diagnostic and therapeutic context of CTP1

• Analysis of the secondary structure of the cys-less yeast mitochondrial citrate transport protein and four single-cys variants by circular dichroism [6].

References