High impact information on PRD1

• The identification of peptides released from peptidase-deficient mitochondria by mass spectrometry indicates a dual function of Mop112 and saccharolysin: they degrade peptides generated upon proteolysis of proteins both in the intermembrane and matrix space and presequence peptides cleaved off by specific processing peptidases in both compartments [1].
• Mercurials and EDTA were found to be potent inhibitors of proteinase yscD activity [2].
• However, there is an additional ORF in S. servazzii between PRD1 and KAR4 that is not homologous to any gene in S. cerevisiae or to genes in other organisms [3].
• Sequence comparison revealed complete identity of the proteinase yscD gene with a recently published open reading frame of yeast chromosome III [4].
• The yeast PRD1 gene, encoding proteinase yscD, was cloned by complementation of the prd1-6 point mutation [4].

Biological context of PRD1

• Diploids heterozygous for PRD1 display gene dosage [5].

Anatomical context of PRD1

• Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria [1].

References