scholarly journals Remodeling of the pioneer translation initiation complex involves translation and the karyopherin importin  

2009 ◽  
Vol 23 (21) ◽  
pp. 2537-2550 ◽  
Author(s):  
H. Sato ◽  
L. E. Maquat
Keyword(s):  
Translation Initiation ◽  
Initiation Complex

scholarly journals UFMylation regulates translational homeostasis and cell cycle progression

2020 ◽  
Author(s):  
Igor A. Gak ◽  
Djordje Vasiljevic ◽  
Thomas Zerjatke ◽  
Lu Yu ◽  
Mario Brosch ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Translation Initiation ◽  
Posttranslational Modification ◽  
Cell Cycle Progression ◽  
Ribosome Profiling ◽  
Biological Functions ◽  
Initiation Complex ◽  
Cycle Progression ◽  
Cellular Targets ◽  
Global Translation

SummaryUFMylation, the posttranslational modification of proteins with ubiquitin fold modifier 1 (UFM1) is essential for metazoan life and is associated with multiple human diseases. Although UFMylation has been linked to endoplasmic reticulum (ER) stress, its biological functions and relevant cellular targets beyond the ER are obscure. Here, we show that UFMylation directly controls translation and cell division in a manner otherwise known for cellular homeostasis-sensing pathways such as mTOR. By combining cell cycle analyses, mass spectrometry and ribosome profiling we demonstrate that UFMylation is required for eIF4F translation initiation complex assembly and recruitment of the ribosome. Interference with UFMylation shuts down global translation, which is sensed by cyclin D1 and halts the cell cycle independently of integrated stress response signalling. Our findings establish UFMylation as a key regulator of translation and uncover a pathway that couples translational homeostasis to cell cycle progression via a ubiquitin-like modification.

scholarly journals Universal scanning-free initiation of eukaryote protein translation–a new normal

2021 ◽  
Vol 12 (1) ◽  
pp. 129-131
Author(s):  
Saranya Auparakkitanon ◽  
Prapon Wilairat
Keyword(s):  
Translation Initiation ◽  
Untranslated Region ◽  
Unique Feature ◽  
Protein Translation ◽  
Initiation Codon ◽  
Initiation Complex ◽  
New Normal ◽  
Free Translation

Abstract A unique feature of eukaryote initiation of protein translation is a so-called scanning of 5′-untranslated region (5′-UTR) by a ribosome initiation complex to enable bound Met-tRNAi access to the initiation codon located further downstream. Here, we propose a universal scanning-free translation initiation model that is independent of 5′-UTR length and applicable to both 5′-m7G (capped) and uncapped mRNAs.

scholarly journals Reversing chemoresistance by small molecule inhibition of the translation initiation complex eIF4F

2010 ◽  
Vol 108 (3) ◽  
pp. 1046-1051 ◽  
Author(s):  
R. Cencic ◽  
D. R. Hall ◽  
F. Robert ◽  
Y. Du ◽  
J. Min ◽  
...  
Keyword(s):  
Small Molecule ◽  
Translation Initiation ◽  
Initiation Complex ◽  
Small Molecule Inhibition

scholarly journals Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association

2016 ◽  
Vol 2 (3) ◽  
pp. e1501502 ◽  
Author(s):  
Thiemo Sprink ◽  
David J. F. Ramrath ◽  
Hiroshi Yamamoto ◽  
Kaori Yamamoto ◽  
Justus Loerke ◽  
...  
Keyword(s):  
Translation Initiation ◽  
Protein Biosynthesis ◽  
Initiation Factor ◽  
Structural Basis ◽  
Initiation Complex ◽  
Cryo Electron Microscopy ◽  
Initiation Factor 2 ◽  
High Resolution Structure ◽  
Guanosine Triphosphatase ◽  
Resolution Structure

Throughout the four phases of protein biosynthesis—initiation, elongation, termination, and recycling—the ribosome is controlled and regulated by at least one specified translational guanosine triphosphatase (trGTPase). Although the structural basis for trGTPase interaction with the ribosome has been solved for the last three steps of translation, the high-resolution structure for the key initiation trGTPase, initiation factor 2 (IF2), complexed with the ribosome, remains elusive. We determine the structure of IF2 complexed with a nonhydrolyzable guanosine triphosphate analog and initiator fMet-tRNAiMet in the context of the Escherichia coli ribosome to 3.7-Å resolution using cryo-electron microscopy. The structural analysis reveals previously unseen intrinsic conformational modes of the 70S initiation complex, establishing the mutual interplay of IF2 and initator transfer RNA (tRNA) with the ribsosome and providing the structural foundation for a mechanistic understanding of the final steps of translation initiation.

scholarly journals The Cryo-EM Structure of a Translation Initiation Complex from Escherichia coli

Cell ◽  
2005 ◽  
Vol 121 (5) ◽  
pp. 703-712 ◽  
Author(s):  
Gregory S. Allen ◽  
Andrey Zavialov ◽  
Richard Gursky ◽  
Måns Ehrenberg ◽  
Joachim Frank
Keyword(s):  
Escherichia Coli ◽  
Translation Initiation ◽  
Initiation Complex
Sign in / Sign up

Export Citation Format

Share Document