Education

PHD, 1982, University of Calcutta
MSC, 1976, University of Calcutta
BSC, 1974, University of Calcutta

Relevant Publications

Pandey, A. K.*, Pain, J.*, Dancis, A. and Pain, D. Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm for iron-sulfur cluster assembly and tRNA thiolation in yeast. Journal of Biological Chemistry, 294: 9489-9502, 2019. *Equal contributions.

Pandey, A., Pain, J., Dziuba, N., Pandey, A. K., Dancis, A., Lindahl, P.A. and Pain, D. Mitochondria export sulfur species required for cytosolic tRNA thiolation. Cell Chemical Biology, 25: 738-748, 2018. A preview/commentary by Joseph J. Braymer and Dennis R. Winge appears in the same issue (Cell Chemical Biology, 25: 645-647, 2018.)

Pain, D. and Dancis, A. Roles of Fe-S proteins: from cofactor synthesis to iron homeostasis to protein synthesis. Current Opinion in Genetics and Development, 38: 45-51, 2016.

Yoon, H., Knight, S. A. B., Pandey, A., Pain, J., Turkarslan, S., Pain, D. and Dancis, A. Turning Saccharomyces cerevisiae into a frataxin-independent organism. PLoS Genetics, 11(5): e1005135. doi:10.1371/journal.pgen.1005135, 2015. A commentary/perspective by Dennis Dean and Patricia Dos Santos appears in the same issue (PLoS Genetics 11(5): e1005192. doi:10.1371/journal.pgen.1005192, 2015.)

Pandey, A., Pain, J., Ghosh, A. K., Dancis, A. and Pain, D. Fe-S cluster biogenesis in isolated mammalian mitochondria: coordinated use of persulfide sulfur and iron and requirements for GTP, NADH, and ATP. Journal of Biological Chemistry, 290, 640-657, 2015.

Pandey, A., Gordon, D. M., Pain, J., Stemmler, T. L., Dancis, A. and Pain, D. Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly. Journal of Biological Chemistry, 288: 36773- 36786, 2013. Selected as 'Paper of the Week'.

Pandey, A., Golla, R., Yoon, H., Dancis, A. and Pain, D. Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis. Biochemical Journal, 448: 171-187, 2012. Highlighted in the 'BJ Spotlight'.

Amutha, B., Gordon, D. M., Dancis, A. and Pain, D. Nucleotide-dependent iron-sulfur cluster biogenesis of endogenous and imported apoproteins in isolated intact mitochondria. Methods in Enzymology, 456: 247-266, 2009.

Mitochondria-cytoplasm interactions for cytosolic iron-sulfur cluster assembly and tRNA thiolation

Iron-sulfur (Fe-S) clusters are critical protein cofactors required for essential cellular processes such
as respiration, ribosome biogenesis, and DNA metabolism. Likewise, tRNA thiolation is needed for
efficient protein synthesis, prevention of protein misfolding, and sensing of cellular sulfur availability.
We found that isolated cytoplasm by itself cannot thiolate tRNAs or synthesize Fe-S clusters but can
do so with the addition of mitochondria. Mechanistically, mitochondria synthesize and export two
distinct and non-interchangeable intermediates, Sint and (Fe-S)int, to the cytoplasm for tRNA
thiolation and Fe-S cluster assembly, respectively. Our goal is to delineate mitochondrial
contributions to these cytoplasmic processes. This includes biochemical characterization and
elucidation of the chemical nature of the intermediates. The results may identify a vital mitochondria-
cytoplasm interaction required for cell survival.