scholarly journals Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex

2012 ◽  
Vol 40 (18) ◽  
pp. 9319-9328 ◽  
Author(s):  
Kan Kobayashi ◽  
Kazuki Saito ◽  
Ryuichiro Ishitani ◽  
Koichi Ito ◽  
Osamu Nureki
Keyword(s):  
Translation Termination ◽  
Structural Basis

Structural basis for ArfA–RF2-mediated translation termination on mRNAs lacking stop codons

Nature ◽  
2016 ◽  
Vol 541 (7638) ◽  
pp. 546-549 ◽  
Author(s):  
Paul Huter ◽  
Claudia Müller ◽  
Bertrand Beckert ◽  
Stefan Arenz ◽  
Otto Berninghausen ◽  
...  
Keyword(s):  
Translation Termination ◽  
Structural Basis ◽  
Stop Codons

Structural basis for translation termination on the 70S ribosome

Nature ◽  
2008 ◽  
Vol 454 (7206) ◽  
pp. 852-857 ◽  
Author(s):  
Martin Laurberg ◽  
Haruichi Asahara ◽  
Andrei Korostelev ◽  
Jianyu Zhu ◽  
Sergei Trakhanov ◽  
...  
Keyword(s):  
Translation Termination ◽  
Structural Basis ◽  
70S Ribosome

scholarly journals Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus

2016 ◽  
Vol 7 (1) ◽  
Author(s):  
Xuhua Tang ◽  
Yiping Zhu ◽  
Stacey L. Baker ◽  
Matthew W. Bowler ◽  
Benjamin Jieming Chen ◽  
...  
Keyword(s):  
Murine Leukemia Virus ◽  
Translation Termination ◽  
Leukemia Virus ◽  
Moloney Murine Leukemia Virus ◽  
Structural Basis ◽  
Murine Leukemia

scholarly journals Structural basis for selective stalling of human ribosome nascent chain complexes by a drug-like molecule

2018 ◽  
Author(s):  
Wenfei Li ◽  
Fred R. Ward ◽  
Kim F. McClure ◽  
Stacey Tsai-Lan Chang ◽  
Elizabeth Montabana ◽  
...  
Keyword(s):  
Small Molecules ◽  
Translation Termination ◽  
Structural Basis ◽  
Small Subset ◽  
Peptidyl Transferase ◽  
Peptidyl Transferase Center ◽  
Chain Complexes ◽  
Nascent Chain ◽  
Exit Tunnel ◽  
Ribosome Exit Tunnel

AbstractSmall molecules that target the ribosome generally have a global impact on protein synthesis. However, the drug-like molecule PF-06446846 (PF846) binds the human ribosome and selectively blocks the translation of a small subset of proteins by an unknown mechanism. In high-resolution cryo-electron microscopy (cryo-EM) structures of human ribosome nascent chain complexes stalled by PF846, PF846 binds in the ribosome exit tunnel in a newly-identified and eukaryotic-specific pocket formed by the 28S ribosomal RNA (rRNA), and redirects the path of the nascent polypeptide chain. PF846 arrests the translating ribosome in the rotated state that precedes mRNA and tRNA translocation, with peptidyl-tRNA occupying a mixture of A/A and hybrid A/P sites, in which the tRNA 3’-CCA end is improperly docked in the peptidyl transferase center. Using mRNA libraries, selections of PF846-dependent translation elongation stalling sequences reveal sequence preferences near the peptidyl transferase center, and uncover a newly-identified mechanism by which PF846 selectively blocks translation termination. These results illuminate how a small molecule selectively stalls the translation of the human ribosome, and provides a structural foundation for developing small molecules that inhibit the production of proteins of therapeutic interest.

scholarly journals The Structural Basis for Release Factor Activation during Translation Termination Revealed by Time-Resolved Cryogenic Electron Microscopy

2019 ◽  
Vol 116 (3) ◽  
pp. 574a-575a ◽  
Author(s):  
Ziao Fu ◽  
Gabriele Indrisiunaite ◽  
Sandip Kaledhonkar ◽  
Binita Shah ◽  
Ming Sun ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Translation Termination ◽  
Structural Basis ◽  
Release Factor ◽  
Time Resolved

Structural basis of translation termination, rescue, and recycling in mammalian mitochondria

2021 ◽  
Author(s):  
Eva Kummer ◽  
Katharina Noel Schubert ◽  
Tanja Schoenhut ◽  
Alain Scaiola ◽  
Nenad Ban
Keyword(s):  
Translation Termination ◽  
Structural Basis ◽  
Mammalian Mitochondria

scholarly journals Structural Basis for Translation Termination on a Pseudouridylated Stop Codon

2016 ◽  
Vol 428 (10) ◽  
pp. 2228-2236 ◽  
Author(s):  
Egor Svidritskiy ◽  
Rohini Madireddy ◽  
Andrei A. Korostelev
Keyword(s):  
Stop Codon ◽  
Translation Termination ◽  
Structural Basis

Organization of tight junctions in the choroid plexus epithelium

1978 ◽  
Vol 36 (2) ◽  
pp. 336-337
Author(s):  
B. Van Deurs ◽  
J. K. Koehler
Keyword(s):  
Choroid Plexus ◽  
Present Report ◽  
Freeze Fracture ◽  
Barrier Properties ◽  
Cell Junctions ◽  
Structural Basis ◽  
Apical Surface ◽  
Choroid Plexus Epithelium ◽  
Solid Nitrogen ◽  
Special Composition

The choroid plexus epithelium constitutes a blood-cerebrospinal fluid (CSF) barrier, and is involved in regulation of the special composition of the CSF. The epithelium is provided with an ouabain-sensitive Na/K-pump located at the apical surface, actively pumping ions into the CSF. The choroid plexus epithelium has been described as “leaky” with a low transepithelial resistance, and a passive transepithelial flux following a paracellular route (intercellular spaces and cell junctions) also takes place. The present report describes the structural basis for these “barrier” properties of the choroid plexus epithelium as revealed by freeze fracture.Choroid plexus from the lateral, third and fourth ventricles of rats were used. The tissue was fixed in glutaraldehyde and stored in 30% glycerol. Freezing was performed either in liquid nitrogen-cooled Freon 22, or directly in a mixture of liquid and solid nitrogen prepared in a special vacuum chamber. The latter method was always used, and considered necessary, when preparations of complementary (double) replicas were made.

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