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
EEA | Norway Grants| NCN
Link to the project page in Polish: PL
Events and news from the project are published in the NEWS section:
2023-05-11 Katarzyna's research in the spotlight
2023-01-09 Visit of schoolchildren from Liceum Sobieskiego in Lublin, Poland - Katarzyna talked about her research.
2022-11-30 Katarzyna receives L'Oréal-UNESCO Scholarship
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