Samrat Mukhopadhyay

Happy to share that after a long-drawn-out process, my institute has removed the first word of my academic rank. First time in my academic life, I have got a "one-word" description of my position. I thank my incredible students for their contributions and my family for support.😀

Captured here is the true heart of 🧬RIM 2026🧬—a vibrant community united by a collective passion for uncovering the mysteries of the transcriptome. Standing together, this group photo represents the incredible diversity and brilliance that defined our meeting.

Today I'll be speaking at the Jawaharlal Nehru Centre For Advanced Scientific Research (JNCASR), Bangalore. If you are at JNCASR and want to attend my seminar, it is at 11 AM in Kanada Auditorium. See you!

Looking forward to attending and speaking at the RNA India Meeting that will be held in April at the Indian Institute of Science, Bangalore. Should be fun to learn from leading RNA biologists and to speak about our new studies on the phase separation of RNA-binding proteins.

Bacteria are full of diverse molecular tricks. This Science article reports an interesting one that is being misrepresented by news coverage, including the coverage in Science. The study describes an enzyme complex that synthesizes alternating dinucleotide repeat DNA as part of an immune response. Protein templating DNA is a cool observation, even if the sequence is only a repeating dinucleotide. The headline-grabbing takeaway is the mechanism of the Drt3b subunit. While its partner, Drt3a, uses a canonical RNA template (reverse transcription), Drt3b synthesizes the complementary strand in the absence of a nucleic acid template. Instead, it uses specific amino acid residues (a glutamate and an arginine) to stabilize and "select" the incoming dNTPs. It is tempting to view this as a radical shift in our understanding of information transfer, a "protein-templated" genetic sequence. However, we should be cautious with the "paradigm shift" narrative. Why this isn't "rewriting" the Genetic Code: Despite claims in the news coverage, this finding does not represent a new form of hereditary information transfer. This is not a protein "reading" itself to create a complex message; rather, it is a highly specialized structural constraint. The protein is essentially a "stuttering" machine, physically keyed to produce a simple, repetitive sequence. The "information" is hard-coded into the protein's fold to perform a single, specific defensive task, rather than acting as a general-purpose template for diverse genetic messages. The Parallel to tmRNA: This observation is not entirely unprecedented when we look at how bacteria handle biochemical "dead ends." It reminds me of transfer-messenger RNA (tmRNA). In trans-translation, when a ribosome stalls on a broken mRNA, the tmRNA molecule steps in to provide both the tRNA component and a short mRNA "tag" to rescue the ribosome: - The "Non-Standard" Template: Much like tmRNA provides an external sequence to fix a stalled process, the DRT3 ncRNA and the Drt3b protein provide "internal" instructions to create DNA where no genomic template exists. - Specialized Rescue: Both mechanisms are niche "emergency" responses, one for proteostasis (tmRNA) and one for viral defense (DRT3). In the end, this discovery doesn't replace our understanding of the genetic code; it expands the "toolbox" of how cells can synthesize polynucleotides when the standard rules don't apply. It is a beautiful reminder that in the microbial world, if a chemical shortcut is possible, evolution has likely found it.

A stunning view from our on-campus apartment at IISER Mohali: Churdhar Peak (11,965 ft), after fresh snowfall, is visible from here (coldest April in several decades!). I clicked a few pictures from our apartment balcony and our guest house terrace.