We use molecular biology, genetics, and biochemistry approaches in the budding yeast
Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe to study
functions of proteins related to ubiquitin in cell division, pre-mRNA splicing, heterochromatin
formation and intracellular trafficking. A few ongoing projects are listed below:
Ubiquitin-like proteins in intron-specific splicing and alternative splicing: The process of
pre-mRNA splicing through spliceosome is understood well. Its regulation is essential for
intron-specific splicing and alternative splicing. We study the role of the ubiquitin-like
proteins Hub1 and Sde2 in these processes.
Molecular evolution of the ubiquitin fold in Sde2: Multiple evidence suggests that the
ubiquitin fold in the intron-specific pre-mRNA splicing factor Sde2 likely originated from
ubiquitin. Can its origin be traced through experiments?
Function of AAA-ATPases: These enzymes are known to play modulatory roles in a large
number of cellular machineries. We study their role in cell division.
Intracellular signalling from Golgi to the nucleus: How Golgi communicates with the
nucleus? Is this communication mediated via intron-specific splicing, and whether
ubiquitin-like proteins and deubiquitinating enzymes (DUBs) participate in the signalling?
We study the roles of these molecules in the trafficking and degradation of transporters
of nutrients, such as glucose and phosphate.
Deubiquitinating enzymes (DUBs) in cellular trafficking: The reversible process of
ubiquitination plays a central role in regulating vesicular trafficking in the cell. Although
the activities of E3 ubiquitin ligases that attach ubiquitin to protein substrates are well
documented, the roles of DUBs that remove ubiquitin are yet to be studied.
Sajeevan A, Pandian R, Mishra SK
2022,
Vectors with a flexible multiple cloning site and modular epitope tags for gene expression studies in Schizosaccharomyces pombe.
Gene Reports
Varikkapulakkal A, Ghosh A, Mishra SK
2022,
Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors.
micropublication Biology