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Background  Cellular oxygen sensing is fundamental to all mammalian cells to adequately respond to a shortage of oxygen by increasing the expression of genes that will ensure energy homeostasis. The transcription factor Hypoxia-Inducible-Factor-1 (HIF-1) is the key regulator of the response because it coordinates the expression of hypoxia inducible genes. The abundance and activity of HIF-1 are controlled through posttranslational modification by hydroxylases, the cellular oxygen sensors, of which the activity is oxygen dependent.    Methods  Fluorescence resonance energy transfer (FRET) was established to determine the assembly of the HIF-1 complex and to study the interaction of the α-subunit of HIF-1 with the O 2 -sensing hydroxylase. New software was developed to improve the quality and reliability of FRET measurements.    Results  FRET revealed close proximity between the HIF-1 subunits in multiple cells. Data obtained by sensitized FRET in this study were fully compatible with previous work using acceptor bleaching FRET. Interaction between the O 2 -sensing hydroxylase PHD1 and HIF-1α was demonstrated and revealed exclusive localization of O 2 -sensing in the nucleus. The new software  FRET  significantly improved the quality and speed of FRET measurements.    Conclusion  FRET measurements do not only allow following the assembly of the HIF-1 complex under hypoxic conditions but can also provide important information about the process of O 2 -sensing and its localisation within a cell.   MCS codes:  92C30, 92C05, 92C40

Nanoscopy of the cellular response to hypoxia by means of fluorescence resonance energy transfer (FRET) and new FRET software