Dynamic alternation of three-dimensional (3D) architecture of chromatin and their spatial repositioning regulate many nuclear processes such as replication, DNA repair, gene expression, mRNA export etc. However, the underlying mechanism of chromatin architectural alteration has remained unexplored. Recently, our lab has uncovered a remarkable phenomenon of dynamic alternation of Heat Shock Protein (HSP) genes conformation upon their transcriptional activation, that is regulated by the heat shock transcription factor 1(Hsf1), in response to heat stress. Moreover, our lab and others have also observed that upon heat stress heat shock protein genes can reposition to the nuclear periphery. Studies from Jason H Brickner lab (JCB 2016) reported that inducible genes reposition and engage in inter-chromosomal clustering at the nuclear periphery and this is mediated by the interaction between transcription factors and nuclear pore complex protein(s). Furthermore, a previous study by Schneider et al. Cell (2015) showed that the nuclear pore-associated TREX2 complex can regulate gene expression by repositioning Mediator to nuclear pore complex. Therefore, my present research is focused on unveiling the answers to questions such as: does the coalescence phenomenon that we observe for HSP genes require nuclear repositioning of the genes to the NPC or is this phenomenon uncoupled with nuclear pore complex re-localization? Which factors are involved in this process? Unpublished observations of our lab suggest that Mediator might be involved in the coalescence of HSP gene upon heat shock. Does the interaction between Mediator and nuclear pore complex proteins actively participate in the HSP gene coalescence in response to heat shock?