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Deepak T. Nair

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Indian academic (born 1973)

Deepak T. Nair
Prof . Deepak T. Nair
Born (1973-10-25)25 October 1973 (age 52)
Pune, India
Alma mater
Known forStudies onDNA polymerases andRNA polymerases
Awards
Scientific career
Fields
Institutions

Deepak Thankappan Nair (born 25 October 1973) is an Indian Structural Biologist and a scientist at theRegional Centre for Biotechnology. He is known for his studies onDNA andRNA polymerases. Deepak was a Ramanujan fellow of theScience and Engineering Research Board (2008–2013) and a recipient of theNational BioScience Award for Career Development (Dept of Biotechnology). TheCouncil of Scientific and Industrial Research, the apex agency of the Government of India for scientific research, awarded him theShanti Swarup Bhatnagar Prize for Science and Technology, one of the highest Indian science awards, for his contributions to biological sciences in 2017.[1][note 1][2] He was inducted as a fellow of the Indian National Science Academy (New Delhi, India) in December 2022. The Haryana government awarded him the Haryana Vigyan Ratna Award for the year 2024.[3]

Biography

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University of Pune

His parents are from the southern state ofKerala, and he was born in Pune in the western state of Maharashtra on 25 October 1973.[4] Deepak Nair attended the Jai Hind High School (Pimpri) and later went to the St. Vincent's Junior College (Pune). He graduated with a BSc in chemistry from Fergusson College (1994) and completed his master's in biotechnology from theSavitribai Phule Pune University (1996).[5] Subsequently, he enrolled for his doctoral studies at theNational Institute of Immunology, India, to secure a PhD in structural immunology in 2001. For his PhD, he worked under the supervision of Dr.Dinakar Mashnu Salunke. Later, he moved to the US to complete his post-doctoral work in Prof. Aneel K. Aggarwal's laboratory at theMount Sinai Medical Center. He returned to India in 2007 to take up the position of an independent investigator at theNational Centre for Biological Sciences.[6] He worked in NCBS as Reader-F (2007–2013) and associate professor (2013–2014). In July 2014, he joined theRegional Centre for Biotechnology as an associate professor and was promoted to professor in July 2019.[5]

Research

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Deepak Nair has obtained new insight regarding the molecular mechanisms that determine the fidelity of the replication process in bacteria and flaviviruses. Recently, his laboratory contributed towards our understanding of DNA mismatch Repair in prokaryotes.[7] His laboratory has shed new light on the strategy utilized by DNA polymerases to prevent ribonucleotide incorporation.[8] In 2018, his laboratory showed that pyrophosphate hydrolysis is an intrinsic and critical step in the DNA synthesis reaction catalyzed by DNA polymerases, and this discovery was accorded breakthrough status by the journal Nucleic Acids Chemistry.[9] Regarding the piggyBac transposase, his laboratory has shown that the dimerization through the Ring Finger Domain present at the C-terminus attenuates the excision activity of this enzyme.[10] He has discovered the mechanism employed by DNA polymerase IV to rescue replication stalled at damaged nucleotides with unprecedented efficiency and accuracy.[11] Nair has provided insight into how specialized DNA polymerases that participate in adaptive mutagenesis ensure the achievement of function.[12][13][14] His laboratory has shown how GTP binding to the viral RNA-dependent-RNA polymerase ensures accurate initiation of replication of the viral genome (Nucleic Acids Research, 2014, 42:2758–2573). In addition, he has shown that reactive oxygen species play an important role in the antimicrobial activity of bactericidal antibiotics (Angew Chem Int Ed Engl. 2016 55:2397-400). In collaboration with D. N. Rao (Department of Biochemistry, IISc), his laboratory has also contributed towards understanding how proteins involved in the post-replicative repair of DNA mismatches function.[15][16] His laboratory has shown that the proofreading domain of the Pfprex DNA polymerase from Plasmodium falciparum is capable of removing misincorporated oxidized nucleotides from the primer[17] and translesion DNA synthesis past common oxidized template nucleotides.[18] Recently, his laboratory has helped characterize a monoclonal antibody that can neutralize different Variants-of-Concern of the SARS-CoV-2 virus.[19] Using computational tools, his laboratory has also identified possible inhibitors of the RNA-dependent-RNA polymerase (IUBMB Life, 2020, 72:2112) and proofreading exoribonuclease from SARS-CoV-2.[20] His laboratory also provided the structure of P4A2, a broadly neutralizing anti-SARS-CoV-2 mAb, in complex with the Receptor-Binding-Domain of the Spike protein.[19] So far, he has been centrally involved in the deposition of 76 entries in the protein data bank, a repository of three-dimensional structures of biological macromolecules.

As a post-doctoral fellow (Dec 2001 – July 2007), he focused on understanding the structural basis of DNA lesion bypass by eukaryotic Y-family DNA polymerases using X-ray crystallography. Due to the action of various agents, lesions are formed on DNA, which interfere with normal replication and may also prove carcinogenic. Eukaryotes possess up to four specialized DNA polymerases that can synthesize DNA across these lesions and thus prevent the replication fork from stalling. Nair determined the crystal structure of the catalytic cores of two such polymerases, human DNA polymerase iota (hPolι) and yeast REV1 (yREV1) –in complex with DNA and incoming nucleotide. The structures of hPolι and yRev1 in complex with undamaged and damaged DNA has shown that these two polymerases prefer altered modes of base-pairing in the active site to facilitate lesion bypass;.[21][22][23][24][25][26][27] Both hPolι and yREV1 have unique active sites that facilitate the formation of non-Watson-Crick base pairs to achieve lesion bypass and rescue stalled replication. He also played a role in determining the structure of a third Y-family polymerase, human DNA Polymerase kappa, in its functional state.[28] In addition, he also participated in projects aimed at understanding the nature of interactions between the translational regulator Pumilio and non-cognate RNA targets[29] and discerning the preference of hPolι for incorporating dGTP when the base of the templating nucleotide is thymine.[30]

His doctoral thesis (July 1996 – Dec 2001) describes the crystallographic analysis of a panel of three murine monoclonal antibodies raised against the same promiscuous peptide antigen PS1 (HQLDPAFGANSTNPD).[31][32] The comparison of the structure of the antibodies in their bound and unbound state suggests there could be a convergence of both epitope and paratope conformations in an antibody response against a flexible immunodominant epitope.[32] He also carried out a computational analysis of the conformational propensities of native and retro-inverso versions of B-cell and T-cell epitopes.[33] This study showed that conformational and functional mimicry can be achieved through retro-inversion only if the native peptide is present in a linear extended conformation in its functional state. He was also involved in the structure determination of an antibacterial protein from tasar silkwormAntheraea mylitta.[34] In addition, he modeled the complex of the ribonuclease restriction and its rRNA substrate.[35]

Awards and honors

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Deepak T. Nair was selected for the Ramanujan Fellowship by theDepartment of Biotechnology for 2008–2013.[6] He became a member of theGuha Research Conference in 2013. He received theNational Bioscience Award for Career Development (N-BIOS Prize) in 2014.[36] The Council of Scientific and Industrial Research awarded him theShanti Swarup Bhatnagar Prize, one of the highest Indian science awards, in 2017.[2] In 2018, he became a laureate of theAsian Scientist 100 by theAsian Scientist (Recognizing Scientific Excellence With The Asian Scientist 100 – Asian Scientist Magazine). He was inducted as a fellow of the Indian National Science Academy (New Delhi, India) in December 2022. The Haryana state government awarded him the Haryana Vigyan Ratna Award for the year 2024.

Academic Activities

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Deepak T. Nair is the course coordinator and instructor for the Molecular Biology & Genetic Engineering (RCB303) and Methods in Molecular Biology (RCB306) courses at the Regional Centre for Biotechnology. He is part of the Academic Management Committee at RCB and the coordinator of the Data Science module for the practical course conducted for the students of the RCB-BRIC-PhD and the Postgraduate Diploma in Biotechnology (PGDIB) programs.

Resources for Indian Science

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At RCB, Deepak T. Nair has participated in the development and management of national resources for Indian Science. He was the primary coordinator of the ESRF access program of RCB, funded by the DBT, that enabled Indian researchers to access the structural biology resources at the European Synchrotron Radiation Facility (https://esrf.rcb.res.in). The program was inaugurated by the then Minister for Science & Technology, Dr.Harsh Vardhan H, in June 2017 and was closed in January 2024. The ESRF access program of the DBT helped nearly 200 researchers- mostly PhD students- from India publish about 240 research papers in international peer-reviewed journals. Deepak is now centrally involved in the management of the Advanced Technology Platform Centre, that provides paid services at the Electron Microscopy, Genomics, Molecular Interactions, Optical Microscopy, and Protein Expression facilities to researchers from all over India (https://atpc.rcb.res.in). He also participated in the development and management of the Indian Biological Data Centre, which will serve as a digital repository for all research data generated in the area of Life Sciences (https://ibdc.dbtindia.gov.in/).

Notes

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  1. ^Long link – please select award year to see details

References

[edit]
  1. ^"View Bhatnagar Awardees". Shanti Swarup Bhatnagar Prize. 2017. Retrieved11 November 2017.
  2. ^ab"10 scientists receive Shanti Swarup Bhatnagar Prize".The Hindu. 26 September 2017. Retrieved11 November 2017.
  3. ^"State govt announces Vigyan Ratna Awards for scientists".The Tribune. Retrieved28 July 2025.
  4. ^"Brief Profile of the Awardee". Shanti Swarup Bhatnagar Prize. 21 October 2017. Retrieved21 October 2017.
  5. ^ab"Biographical Information – Deepak Nair".Regional Centre for Biotechnology. 9 November 2017. Archived fromthe original on 5 November 2017. Retrieved9 November 2017.
  6. ^ab"Profile on SERB"(PDF).Science and Engineering Research Board. 14 November 2017. Retrieved14 November 2017.
  7. ^Nirwal, Shivlee; Jha, Ritika; Narayanan, Naveen; Sharma, Minakshi; Kulkarni, Dhananjaya S; Sharma, Dalchand; Babu, Amith S; Suthar, Dhiraj K; Rao, Desirazu N; Nair, Deepak T (2025)."The structure of the MutL-CTD:processivity-clamp complex provides insight regarding strand discrimination in non-methyl-directed DNA mismatch repair".Nucleic Acids Research.53 (4) gkaf094.doi:10.1093/nar/gkaf094.PMC 11840563.PMID 39988319.
  8. ^Johnson, Mary K; Kottur, Jithesh; Nair, Deepak T (2019)."A polar filter in DNA polymerases prevents ribonucleotide incorporation".Nucleic Acids Research.47 (20):10693–10705.doi:10.1093/nar/gkz792.PMC 6846668.PMID 31544946.
  9. ^Kottur, Jithesh; Nair, Deepak T (2018)."Pyrophosphate hydrolysis is an intrinsic and critical step of the DNA synthesis reaction".Nucleic Acids Research.46 (12):5875–5885.doi:10.1093/nar/gky402.PMC 6159520.PMID 29850882.
  10. ^Sharma, Rahul; Nirwal, Shivlee; Narayanan, Naveen; Nair, Deepak T. (2018). "Dimerization through the RING-Finger Domain Attenuates Excision Activity of the piggyBac Transposase".Biochemistry.57 (20):2913–2922.doi:10.1021/acs.biochem.7b01191.PMID 29750515.
  11. ^Kottur, Jithesh; Sharma, Amit; Gore, Kiran R.; Narayanan, Naveen; Samanta, Biswajit; Pradeepkumar, Pushpangadan I.; Nair, Deepak T. (2015). "Unique Structural Features in DNA Polymerase IV Enable Efficient Bypass of the N 2 Adduct Induced by the Nitrofurazone Antibiotic".Structure.23 (1):56–67.doi:10.1016/j.str.2014.10.019.PMID 25497730.
  12. ^Sharma, Amit; Kottur, Jithesh; Narayanan, Naveen; Nair, Deepak T. (2013)."A strategically located serine residue is critical for the mutator activity of DNA polymerase IV from Escherichia coli".Nucleic Acids Research.41 (9):5104–5114.doi:10.1093/nar/gkt146.PMC 3643571.PMID 23525461.
  13. ^Sharma, Amit; Subramanian, Vidya; Nair, Deepak T. (2012). "The PAD region in the mycobacterial DinB homologue MsPolIV exhibits positional heterogeneity".Acta Crystallographica Section D Biological Crystallography.68 (8):960–967.doi:10.1107/s0907444912017623.PMID 22868761.
  14. ^Sharma, Amit; Nair, Deepak T. (2012)."MsDpo4—a DinB Homolog fromMycobacterium smegmatis—Is an Error-Prone DNA Polymerase That Can Promote G:T and T:G Mismatches".Journal of Nucleic Acids.2012:1–8.doi:10.1155/2012/285481.PMC 3317225.PMID 22523658.
  15. ^Nirwal, Shivlee; Kulkarni, Dhananjaya S; Sharma, Amit; Rao, Desirazu N; Nair, Deepak T (2018)."Mechanism of formation of a toroid around DNA by the mismatch sensor protein".Nucleic Acids Research.46 (1):256–266.doi:10.1093/nar/gkx1149.PMC 5758902.PMID 29182773.
  16. ^Namadurai, Sivakumar; Jain, Deepti; Kulkarni, Dhananjay S.; Tabib, Chaitanya R.; Friedhoff, Peter; Rao, Desirazu N.; Nair, Deepak T. (2010)."The C-Terminal Domain of the MutL Homolog from Neisseria gonorrhoeae Forms an Inverted Homodimer".PLOS ONE.5 (10) e13726.Bibcode:2010PLoSO...513726N.doi:10.1371/journal.pone.0013726.PMC 2965676.PMID 21060849.
  17. ^Sharma, Minakshi; Narayanan, Naveen; Nair, Deepak T. (2020)."The proofreading activity of Pfprex from Plasmodium falciparum can prevent mutagenesis of the apicoplast genome by oxidized nucleotides".Scientific Reports.10 11157.doi:10.1038/s41598-020-67853-2.PMC 7341739.PMID 32636411.
  18. ^Sharma, Minakshi; Nair, Deepak T. (2022). "Pfprex fromPlasmodium falciparum can bypass oxidative stress-induced DNA lesions".The FEBS Journal.289 (17):5218–5240.doi:10.1111/febs.16414.PMID 35220686.
  19. ^abAhmad Parray, Hilal; Narayanan, Naveen; Garg, Sonal; Abbas Rizvi, Zaigham; Shrivastava, Tripti; Kushwaha, Sachin; Singh, Janmejay; Murugavelu, Praveenkumar; Anantharaj, Anbalagan; Mehdi, Farha; Raj, Nisha; Singh, Shivam; Dandotiya, Jyotsna; Lukose, Asha; Jamwal, Deepti; Kumar, Sandeep; Chiranjivi, Adarsh K.; Dhyani, Samridhi; Mishra, Nitesh; Kumar, Sanjeev; Jakhar, Kamini; Sonar, Sudipta; Kumar Panchal, Anil; Ranjan Tripathy, Manas; Roy Chowdhury, Shirlie; Ahmed, Shubbir; Samal, Sweety; Mani, Shailendra; Bhattacharyya, Sankar; Das, Supratik; Sinha, Subrata; Luthra, Kalpana; Batra, Gaurav; Sehgal, Devinder; Medigeshi, Guruprasad R.; Sharma, Chandresh; Awasthi, Amit; Kumar Garg, Pramod; Nair, Deepak T.; Kumar, Rajesh (2022)."A broadly neutralizing monoclonal antibody overcomes the mutational landscape of emerging SARS-CoV-2 variants of concern".PLOS Pathogens.18 (12) e1010994.doi:10.1371/journal.ppat.1010994.PMC 9779650.PMID 36508467.
  20. ^Narayanan, Naveen; Nair, Deepak T. (2021)."Ritonavir may inhibit exoribonuclease activity of nsp14 from the SARS-CoV-2 virus and potentiate the activity of chain terminating drugs".International Journal of Biological Macromolecules.168:272–278.doi:10.1016/j.ijbiomac.2020.12.038.PMC 7724963.PMID 33309661.
  21. ^Nair, Deepak T.; Johnson, Robert E.; Prakash, Satya; Prakash, Louise; Aggarwal, Aneel K. (2004). "Replication by human DNA polymerase-ι occurs by Hoogsteen base-pairing".Nature.430 (6997):377–380.doi:10.1038/nature02692.PMID 15254543.
  22. ^Nair, D. T. (2005). "Rev1 Employs a Novel Mechanism of DNA Synthesis Using a Protein Template".Science.309 (5744):2219–2222.doi:10.1126/science.1116336.PMID 16195463.
  23. ^Nair, Deepak T.; Johnson, Robert E.; Prakash, Louise; Prakash, Satya; Aggarwal, Aneel K. (2005). "Human DNA Polymerase ι Incorporates dCTP Opposite Template G via a G.C+ Hoogsteen Base Pair".Structure.13 (10):1569–1577.doi:10.1016/j.str.2005.08.010.PMID 16216587.
  24. ^Nair, Deepak T.; Johnson, Robert E.; Prakash, Louise; Prakash, Satya; Aggarwal, Aneel K. (2006). "An Incoming Nucleotide Imposes an anti to syn Conformational Change on the Templating Purine in the Human DNA Polymerase-ι Active Site".Structure.14 (4):749–755.doi:10.1016/j.str.2006.01.010.PMID 16615915.
  25. ^Nair, Deepak T; Johnson, Robert E; Prakash, Louise; Prakash, Satya; Aggarwal, Aneel K (2006). "Hoogsteen base pair formation promotes synthesis opposite the 1,N6-ethenodeoxyadenosine lesion by human DNA polymerase ι".Nature Structural & Molecular Biology.13 (7):619–625.doi:10.1038/nsmb1118.PMID 16819516.
  26. ^Nair, Deepak T.; Johnson, Robert E.; Prakash, Louise; Prakash, Satya; Aggarwal, Aneel K. (2008). "Protein-Template-Directed Synthesis across an Acrolein-Derived DNA Adduct by Yeast Rev1 DNA Polymerase".Structure.16 (2):239–245.doi:10.1016/j.str.2007.12.009.PMID 18275815.
  27. ^Nair, Deepak T.; Johnson, Robert E.; Prakash, Louise; Prakash, Satya; Aggarwal, Aneel K. (2009)."DNA Synthesis across an Abasic Lesion by Human DNA Polymerase ι".Structure.17 (4):530–537.doi:10.1016/j.str.2009.02.015.PMC 2703454.PMID 19368886.
  28. ^Lone, Samer; Townson, Sharon A.; Uljon, Sacha N.; Johnson, Robert E.; Brahma, Amrita; Nair, Deepak T.; Prakash, Satya; Prakash, Louise; Aggarwal, Aneel K. (2007). "Human DNA Polymerase κ Encircles DNA: Implications for Mismatch Extension and Lesion Bypass".Molecular Cell.25 (4):601–614.doi:10.1016/j.molcel.2007.01.018.PMID 17317631.
  29. ^Gupta, Yogesh K.; Nair, Deepak T.; Wharton, Robin P.; Aggarwal, Aneel K. (2008). "Structures of Human Pumilio with Noncognate RNAs Reveal Molecular Mechanisms for Binding Promiscuity".Structure.16 (4):549–557.doi:10.1016/j.str.2008.01.006.PMID 18328718.
  30. ^Jain, Rinku; Nair, Deepak T.; Johnson, Robert E.; Prakash, Louise; Prakash, Satya; Aggarwal, Aneel K. (2009)."Replication across Template T/U by Human DNA Polymerase-ι".Structure.17 (7):974–980.doi:10.1016/j.str.2009.04.011.PMC 3030472.PMID 19604477.
  31. ^Nair, Deepak T; Singh, Kavita; Sahu, Naresh; Rao, Kanury V S; Salunke, Dinakar M (2000). "Crystal Structure of an Antibody Bound to an Immunodominant Peptide Epitope: Novel Features in Peptide-Antibody Recognition".The Journal of Immunology.165 (12):6949–6955.doi:10.4049/jimmunol.165.12.6949.PMID 11120821.
  32. ^abNair, D. T. (2002). "Epitope Recognition by Diverse Antibodies Suggests Conformational Convergence in an Antibody Response".The Journal of Immunology.168 (5):2371–2382.doi:10.4049/jimmunol.168.5.2371.PMID 11859128.
  33. ^Nair, Deepak T.; Kaur, Kanwal J.; Singh, Kavita; Mukherjee, Paushali; Rajagopal, Deepa; George, Anna; Bal, Vineeta; Rath, Satyajit; Rao, Kanury V. S.; Salunke, Dinakar M. (2003). "Mimicry of Native Peptide Antigens by the Corresponding Retro-Inverso Analogs Is Dependent on Their Intrinsic Structure and Interaction Propensities".The Journal of Immunology.170 (3):1362–1373.doi:10.4049/jimmunol.170.3.1362.PMID 12538696.
  34. ^Jain, Deepti; Nair, Deepak T.; Swaminathan, G. Jawahar; Abraham, E.G.; Nagaraju, J.; Salunke, Dinakar M. (2001)."Structure of the Induced Antibacterial Protein from Tasar Silkworm, Antheraea mylitta".Journal of Biological Chemistry.276 (44):41377–41382.doi:10.1074/jbc.m104674200.PMID 11522783.
  35. ^Nayak, Surendra K.; Bagga, Shveta; Gaur, Deepak; Nair, Deepak T.; Salunke, Dinakar M.; Batra, Janendra K. (2001). "Mechanism of Specific Target Recognition and RNA Hydrolysis by Ribonucleolytic Toxin Restrictocin".Biochemistry.40 (31):9115–9124.doi:10.1021/bi010923m.PMID 11478878.
  36. ^"N-BIOS Prize 2014"(PDF).Department of Biotechnology. 2014. Archived fromthe original(PDF) on 11 May 2021. Retrieved14 November 2017.

External links

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