High impact information on QCR7

• The CRO1 protein exhibits significant similarity to the SHE4 protein, which is required for asymmetric mating-type switching in budding yeast cells [1].
• This protein does not contain a cleavable N-terminal mitochondrial targeting sequence, and it is not understood how the Qcr7 protein is imported into mitochondria and assembled into the complex [2].
• In addition, we studied two mutants containing Qcr7 proteins with point mutations in addition to a delta7 truncation, Qcr7p-delta7(D13V) and Qcr7p-delta7(R10K) [2].
• The coding sequence for two highly conserved aspartate residues, D46 and D47, in the QCR7 gene was altered by site-directed mutagenesis and the mutated genes expressed in cells lacking a functional QCR7 gene [3].
• This led to a respiratory-deficient phenotype and drastic decrease in the steady-state levels of Qcr7 (14-kDa) and Qcr8 (11-kDa) proteins [4].

Biological context of QCR7

• The intergenic regions containing the QCR7 promoters of the two yeasts, differ significantly in length and lack overall DNA sequence similarity, but they do share a binding site for the transcription factor complex HAP2/3/4 [5].

Physical interactions of QCR7

• Previous studies have shown that the N-terminus of the Qcr7 protein may be involved in the assembly of the cytochrome bc(1) complex and its C-terminus by interacting with cytochrome b and QCR8 proteins [3].

Other interactions of QCR7

• The chromosomal linkage of the APA2 and QCR7 genes is conserved between S. cerevisiae and K. lactis [5].

References