High impact information on PIR1

• We conclude that Pir1p interacts with Apn1p, at the level of either the cytoplasm or nucleus, and facilitates Apn1p transport into the mitochondria to repair damaged DNA [1].
• Role of Pir1 in the construction of the Candida albicans cell wall [2].
• We isolated three highly homologous genes, PIR1, PIR2 and PIR3, collectively called the PIR genes [3].
• The double disruptants, pir1 pir2, were viable under various conditions, such as higher temperature (37 degrees C) or high salt concentration, but showed a slow-growing phenotype on an agar slab [3].
• We examined the localization of the Pir protein family (Pir1 to Pir4), which is covalently linked to the cell wall in an unknown manner [4].

Biological context of PIR1

• PIR1 and PIR3 are closely linked to each other and are on chromosome XI [3].
• Pir1p mediates translocation of the yeast Apn1p endonuclease into the mitochondria to maintain genomic stability [1].
• Stepwise deletion of the eight units of the repetitive sequence of Pir1p revealed that one unit is enough for the protein to bind bud scars and that the extent of binding of Pir1p to the cell wall depends on the number of these repetitive units [4].

Anatomical context of PIR1

• We found that Pir1p, initially isolated as a cell wall constituent of unknown function, interacts with the C-terminal end of Apn1p, which bears a bipartite nuclear localization signal [1].

Other interactions of PIR1

• Human alpha-1,3-fucosyltansferase (FucT) encoded by the FUT6 gene was displayed at the cell surface of yeast cells engineered using the yeast cell wall protein Pir1 or Pir2, and the FucT activity was detected at the surface of cells producing the Pir1-HA-FUT6 or Pir2-FLAG-FUT6 fusion proteins [5].

Analytical, diagnostic and therapeutic context of PIR1

• Comparison of cell wall localization among Pir family proteins and functional dissection of the region required for cell wall binding and bud scar recruitment of Pir1p [4].

References