ד"ר סאורב מליק

Dr. Saurav (Robb) Mallik joined the faculty of life sciences at Tel Aviv University (TAU) as a Principal Investigator in 2025. Trained initially in physics as an undergraduate at Scottish Church College, Kolkata, India, he transitioned to biology for his master's in molecular biology at the University of Calcutta. His doctoral research, also at the University of Calcutta, investigated the assembly and evolution of protein complexes driven by point mutations. He then moved to the Weizmann Institute of Science, Israel, for his postdoctoral work, focusing on how gene duplication drives the evolution of protein complexes.

2007-2010       Bachelor’s Degree in Physics in the Department of Physics, Scottish Church College, University of Calcutta.
 

2010-2012       Master’s Degree in Biophysics and Molecular Biology in the Department of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta. Thesis Advisor: Prof. Sudip Kundu.
 

2013-2018       Doctoral Research in Structural and Evolutionary Bioinformatics in the Department of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta. Mentor: Prof. Sudip Kundu.
 

2019-2020       Postdoctoral Research in the Department of Biomolecular Sciences, Weizmann Institute of Science. Mentor: Prof. Dan Tawfik.
 

2021-2023       Postdoctoral Research Department of Chemical and Structural Biology, Weizmann Institute of Science. Mentor: Prof. Emmanuel Levy.
 

2023-2025       Research Associate Department of Molecular Genetics, Weizmann Institute of Science. Employer: Prof. Yitzhak Pilpel.

We use evolutionary systems biology to study cell’s functional units: heteromeric protein complexes. These complexes account for over half of all proteins encoded in the genome and exhibit a wide diversity of shape and size. Each complex is composed of a distinct set of subunits. This compositional specificity has long been interpreted as evidence of their static molecular architectures. In reality, protein complexes are compositionally dynamic. Subunit genes can be gained or lost over evolutionary time, silenced across different tissues, or out of synchrony in their expression levels. However, the principles that govern which subunits exhibit this variability and why remain largely unknown.

We focus on two major evolutionary processes that drive compositional change in evolution. First, we examine complex origins (accretion), tracing how present-day multi-subunit complexes originated from simpler ancestral assemblies by incrementally integrating new subunits. Second, we investigate complex simplification (attrition), studying how ancestral multi-subunit heteromeric complexes have been simplified in highly specialized organisms, specifically intracellular symbionts and parasites, through gradual subunit loss.

To address these questions, we combine comparative genomics with large-scale structural quantifications and multi-omics data. Our findings reveal that complexes have evolved to exhibit differential essentiality among their subunits. This evolutionary design elegantly resolves the dilemma of robustness versus evolvability. In accretion, a conserved, invariable core (often catalytic or structurally essential) ensures functional robustness, while compositional changes at the more peripheral, partner-stabilized subunits foster evolvability. In attrition, this same design paves the way for reductive evolution, allowing organisms to retain a minimal functional scaffold while simplifying peripheral components. Taken together, our work bridges comparative genomics, structural biology, and multi-omics to decipher fundamental rules of complex origins and simplification.

Saurav Mallik*, Angel F Cisneros, Christian R Landry*, Emmanuel D Levy* (2025) Co-translational assembly promotes functional diversification of paralogous proteins. BioArxiv, DOI: 10.1101/2025.01.22.634331.

Zikun Zhu, Saurav Mallik, Taylor A Stevens, Riming Huang, Emmanuel D Levy, Shu-ou Shan (2025) Principles of cotranslational mitochondrial protein import. Cell, DOI: 10.1016/j.cell.2025.07.021.

Saurav Mallik*, Johannes Venezian, Arseniy Lobov, Meta Heidenreich, Hector Garcia-Seisdedos, Todd O Yeates, Ayala Shiber*, Emmanuel D Levy* (2025) Structural determinants of co-translational protein complex assembly. Cell, 188(3): 764-777.e22.

Highlighted in Nature Reviews Molecular Cell Biology: https://doi.org/10.1038/s41580-024-00824-x Spotlight in Molecular Cell: https://doi.org/10.1016/j.molcel.2025.01.007

Saurav Mallik*, Dan S Tawfik, Emmanuel D Levy* (2022). Gene Duplication diversifies the Landscape of Protein Oligomeric State and Function. Current Opinion in Genetics and Development, 76: 101966.

Rebeaud M., Mallik S., Goloubinoff P.A., Tawfik D.S. (2020) On the evolution of chaperones and co-chaperones and the expansion of proteomes across the Tree of Life. PNAS 118(21):e2020885118.

Press release: https://wis-wander.weizmann.ac.il/chemistry/cells-and-city

Suman Hait, Saurav Mallik*, Sudipto Basu, Sudip Kundu*. (2019). Finding the generalized molecular principles of protein thermal stability. Proteins, 88(6):788-808.

Saurav Mallik, Dan S. Tawfik* (2020). Determining the interaction status and evolutionary fate of duplicated homomeric proteins. PLoS Computational Biology, 16(8): e1008145.

Faculty Opinions Recommended: facultyopinions.com/prime/738566340

Saurav Mallik & Sudip Kundu* (2018). Topology and oligomerization of mono- and oligomeric proteins regulate their half-lives in the cell. Structure, 26(6): 869–878.

Saurav Mallik & Sudip Kundu* (2017). Coevolutionary constraints in the sequence-space of macromolecular complexes reflect their self-assembly pathways. Proteins, 85(7): 1183-1189

Faculty Opinions Recommended: facultyopinions.com/prime/727450409

Saurav Mallik & Sudip Kundu* (2015). Co-evolutionary constraints of globular proteins correlate with their folding rates. FEBS Letters, 589(17): 2179-85

Faculty Opinions Recommended: facultyopinions.com/prime/725638601

Saurav Mallik, Hiroshi Akashi, Sudip Kundu* (2015). Assembly constraints drive co-evolution among ribosomal constituents, Nucleic Acids Research, 43(11): 5352-5363.