U. Rawat
Howard Hughes Medical Institute
4 Papers
U. Rawat is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Ribosome & Release factor. The author has an hindex of 4, co-authored 4 publications. Previous affiliations of U. Rawat include Wadsworth Center.
Chat about Author
Papers
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.
246
RF3 Induces Ribosomal Conformational Changes Responsible for Dissociation of Class I Release Factors
Haixiao Gao,Zhi-Hong Zhou,U. Rawat,Chenhui Huang,Lamine Bouakaz,Chernhoe Wang,Zhihong Cheng,Yuying Liu,A. Zavialov,Richard Gursky,Suparna Sanyal,Måns Ehrenberg,Joachim Frank,Joachim Frank,Haiwei Song,Haiwei Song +15 more
TL;DR: The crystal structure of E. coli RF3*GDP is presented, which has a three-domain architecture strikingly similar to the structure of EF-Tu*GTP, which shows that a surface region involving domains II and III is important for distinct steps in the action cycle of RF3.
167
Interactions of the release factor RF1 with the ribosome as revealed by cryo-EM
TL;DR: Cryo-electron microscopy results obtained in this study show that ribosome-bound RF1 is in an open conformation, unlike the closed conformation observed in the crystal structure of the free factor, allowing its simultaneous access to both the decoding center and the peptidyl-transferase center.
Locking and unlocking of ribosomal motions.
Mikel Valle,A. Zavialov,Jayati Sengupta,U. Rawat,U. Rawat,Måns Ehrenberg,Joachim Frank,Joachim Frank,Joachim Frank +8 more
TL;DR: During the ribosomal translocation, the binding of elongation factor G to the pretranslocational ribosome leads to a ratchet-like rotation of the 30S sub unit relative to the 50S subunit in the direction of the mRNA movement, implying that this region is involved in the translocation of deacylated tRNAs from the P to the E site.