NISER

1996-2001 : Ph.D. (Molecular Biology) National Institute of Immunology, J.N.U. Campus New Delhi, INDIA 

1994-1996 : M. Sc. (Biochemistry) Department of Biochemistry, Nagpur University, INDIA

1991-1994 : B. Sc. (Microbiology, Biochemistry, Chemistry) Nagpur University, INDIA

Molecular Genetic Study of Protein Biosynthesis

NIH Fellows Award for Research Excellence (NIH-FARE) for years 2005 and 2006.

• Ram, A.K., Kole, T. & Alone, P.V. Translation Initiation Fidelity Defective Mutations in eIF5 and eIF2β Show Distinct Sensitivity to the Sequence Context for Recognition of the UUG Start Codon. Biochem Genet (2025). https://doi.org/10.1007/s10528-025-11312-y
• Gayen A, Alone PV. eIF2β zinc-binding domain interacts with the eIF2γ subunit through the guanine nucleotide binding interface to promote Met-tRNAiMet binding. 2024 Biosci Rep  Jul 31;44(7):BSR20240438. doi: 10.1042/BSR20240438.
• Ram, A.K., Mallik, M., Reddy, R.R. Suryawanshi, AR and Alone PV. Altered proteome in translation initiation fidelity defective eIF5G31R mutant causes oxidative stress and DNA damage. Sci Rep 12, 5033 (2022). https://doi.org/10.1038/s41598-022-08857-y
• Antony A C, Ram AK, Dutta K and Alone PV. Ribosomal mutation in helix 32 of 18S rRNA alters fidelity of eukaryotic translation start site selection. (2019) FEBS Lett.
• Antony A C and Alone PV. Fidelity of HIS4 start codon selection influences 3-amino-1,2,4-triazole sensitivity in GTPase activating protein function defective eIF5. (2018) J Genet. 97 (4): 953-964.
• Antony A C and Alone PV. Defect in the GTPase activating protein (GAP) function of eIF5 causes repression of GCN4 translation. (2017) Biochem Biophys Res Commun. 486 (4):1110-1115.
• Alone PV, Cao C and Dever TE. Translation initiation factor eIF2γ mutants alter start codon selection independent of Met-tRNAiMet binding. (2008) Mol Cell Biol. 28 (22): 6877-88.
• Alone PV and Garg LC. Secretory and GM1 receptor binding role of N-Terminal end of LTB in Vibrio Cholerae. (2008) Biochem Biophy Res Comm. 376 (4): 770-4.
• Alone PV, Malik G, Krishnan A and Garg LC. Deletion mutations in N-terminal α1 helix render heat labile enterotoxin B subunit susceptible to degradation. (2007) Proc Natl Acad Sci (USA). 104 (41): 16056-61
• Alone PV and Dever TE. Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2Bε. (2006) J Biol Chem. 281(18):12636-44.
• Roll-Mecak A, Alone P, Cao C, Dever TE and Burley SK. X-ray structure of translation initiation factor eIF2γ: implications for tRNA and eIF2α binding, (2004) J Biol Chem. 279 (11):10634-42.

My research focuses on understanding eukaryotic translation initiation and its regulation.  We employ biochemical, biophysical and yeast molecular genetics techniques to explore this process. A key process in the central dogma of molecular biology is establishing an open reading frame (ORF) by selecting a start codon to decode the genetic information in mRNA. Some of the key component in this process includes translation initiation factors eIF1, eIF1A, eIF2-GTP-Met-tRNAiMet (ternary complex:TC), eIF5 and 40S ribosome. 

We are interested in understanding the intricacies of eIF2-alpha, eIF2β, Met-tRNAiMet binding to eIF2γ subunit in the TC formation. We showed eIF2γ-domain II interacts with eIF2a subunit, whereas, the eIF2γ has two independent binding sites for eIF2β subunit. Our research indicates the eIF2β binding to eIF2γ site-II near GTP binding interface is flexible. This flexible mechanism enables the eIF2β C-terminal domain to shift position, facilitating the binding of Met-tRNAiMet for the formation of the ternary complex. It then releases Met-tRNAiMet after the start codon is selected. 

eIF5, a GTPase activating protein (GAP), stimulates GTP hydrolysis by the eIF2γ subunit by providing arginine finger. The hydrolysis of GTP by the eIF2γ subunit is a crucial regulatory step in translation initiation. It is closely linked to the selection of the start codon. We are interested in understanding of molecular mechanism of GTP hydrolysis. We demonstrated that the eIF5 N-terminal domain containing the critical arginine finger is both necessary and sufficient for GTP hydrolysis.

The 40S ribosomal subunit provides a platform on which translation initiation factors assembles for the selection of start codon. Our research aims to explore the significance of various regions within the 40S ribosome in the selection of the start codon. We showed that mutation in the helix 32 of 18S rRNA perturbs the head rotation of the 40S ribosome and alters the fidelity of start codon selection. 

Ultimately, the most intriguing aspect lies in understanding the molecular mechanism of non-canonical translation initiation. We’re particularly interested in investigating the selection of non-AUG start codons during this process. Our research focuses on how UUG CUG and ACG codons are utilised and the unique trans-factors or cis-acting RNA sequences required to initiate translation from these codons.  

Ph.D scholars 

• Binayak Mohapatra
• Tanaya Kole
• A. Akhil Kumar
• Soumya Mazumdar

M.Sc Students

• Nikitha Kumaran
• Sumedha Malepati
• Anabell Antony Biju
• Nandini Pal

• Molecular Biology (B304) for MSc students
• Molecular Biology Laboratory (B343) for MSc students
• Advance Molecular Biology (B551/B701) for MSc and Ph.D students