Structural and functional studies of human PNPase in mitochondrial RNA metabolism

Principal Investigator: Katarzyna Bandyra

Human polynucleotide phosphorylase (hPNPase) is a highly conserved exoribonuclease residing mostly in the mitochondrial intermembrane space, where its function is poorly understood. In bacteria, where the enzyme is best understood, PNPase can be re-programmed by the RNA chaperone Hfq and small regulatory RNA (sRNA) to switch from degradative to chaperoning roles in RNA-mediated gene regulation. As the human and bacterial enzymes are homologues, it is possible that hPNPase could have a dual mode of action as well, and could participate in diverse RNA-mediated regulatory processes once trapped in a non-degradative assembly. Our research will address what functions are played by hPNPase present in the intermembrane space of the human mitochondria. We will characterise the full-length enzyme and its capacity to bind substrates in the degradative and non-degradative modes, as well as identify potential hPNPase ternary complexes. In order to achieve these objectives, we will elucidate the structure-function relationship of hPNPase by cryo-EM.

Funding source:

National Science Centre, Poland & EEA and Norway Grants - POLS

Structural and functional studies of human PNPase in mitochondrial RNA metabolism

  • PLN 878 220 (EUR 200 000)
  • Sep 2021 - Aug 2023
  • #2020/37/K/NZ1/02312
  • Project PI: Katarzyna Bandyra

EEA | Norway Grants| NCN

Norway Grants

NCN




Events and news from the project are published in the NEWS section:

2022-09-20 26th Science Festival in Warsaw

2022-09-09 Go!RNA - BANDyra Lab retreat

2022-04-19 A review of bacterial RNA chaperones

2021-09-01 Dr Katarzyna Bandyra joins the lab

2020-12-06 NCN POLS grant to Katarzyna Bandyra