Jayati Sengupta
Indian Institute of Chemical Biology
62 Papers
198 Citations
Jayati Sengupta is an academic researcher from Indian Institute of Chemical Biology. The author has contributed to research in topics: Ribosome & Eukaryotic Ribosome. The author has an hindex of 20, co-authored 57 publications. Previous affiliations of Jayati Sengupta include Academy of Scientific and Innovative Research & Wadsworth Center.
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Papers
Incorporation of Aminoacyl-tRNA into the Ribosome as seen by Cryo-electron Microscopy
Mikel Valle,A. Zavialov,Wen Li,Scott M. Stagg,Jayati Sengupta,Rikke Nielsen,Poul Nissen,Stephen C. Harvey,Måns Ehrenberg,Joachim Frank,Joachim Frank +10 more
TL;DR: A cryo-electron microscopy study presents a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome, and proposes a mechanism to facilitate codon recognition by the incoming aa-tRNA and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu.
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Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process
Mikel Valle,Jayati Sengupta,Neil K. Swami,Robert A. Grassucci,Nils Burkhardt,Knud H. Nierhaus,Rajendra K. Agrawal,Rajendra K. Agrawal,Joachim Frank,Joachim Frank +9 more
TL;DR: Cryo‐ electron microscopy study of an Escherichia coli 70S ribosome‐bound ternary complex stalled with an antibiotic, kirromycin, shows an active role of the tRNA in the transmission of the signal prompting the GTP hydrolysis upon codon recognition.
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Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis
Elizabeth Villa,Jayati Sengupta,Jayati Sengupta,Leonardo G. Trabuco,Jamie LeBarron,William T. Baxter,Tanvir R. Shaikh,Robert A. Grassucci,Poul Nissen,Måns Ehrenberg,Klaus Schulten,Joachim Frank +11 more
TL;DR: The model reveals the conformational changes in the conserved GTPase switch regions ofEF-Tu that trigger hydrolysis of GTP, along with key interactions, including those between the sarcin-ricin loop and the P loop of EF-Tu and a conserved region of the 16S rRNA.
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A cryo-electron microscopic study of ribosome-bound termination factor RF2
U. Rawat,A. Zavialov,Jayati Sengupta,Mikel Valle,Mikel Valle,Robert A. Grassucci,Robert A. Grassucci,Jamie Linde,Bente Vestergaard,Måns Ehrenberg,Joachim Frank,Joachim Frank,Joachim Frank +12 more
TL;DR: It is shown that RF2 is in an open conformation when bound to the ribosome, allowing GGQ to reach the PTC while still allowing SPF–stop-codon interaction, which indicates new interpretations of accuracy in termination, and has implications for how the presence of a stop codon in the DC is signalled to PTC.
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Localization of L11 Protein on the Ribosome and Elucidation of its Involvement in EF-G-dependent Translocation
Rajendra K. Agrawal,Jamie Linde,Jayati Sengupta,Knud H. Nierhaus,Joachim Frank,Joachim Frank,Joachim Frank +6 more
TL;DR: In this paper, the authors determined the position of the complete L11 protein by comparing a three-dimensional cryo-EM reconstruction of the 70 S ribosome, isolated from a mutant lacking ribosomal protein L11, with the 3D map of the wild-type ribosomes.
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