نتایج جستجو برای: eifs

تعداد نتایج: 120  

Journal: :Cell reports 2012
Rafael E Luna Haribabu Arthanari Hiroyuki Hiraishi Jagpreet Nanda Pilar Martin-Marcos Michelle A Markus Barak Akabayov Alexander G Milbradt Lunet E Luna Hee-Chan Seo Sven G Hyberts Amr Fahmy Mikhail Reibarkh David Miles Patrick R Hagner Elizabeth M O'Day Tingfang Yi Assen Marintchev Alan G Hinnebusch Jon R Lorsch Katsura Asano Gerhard Wagner

Recognition of the proper start codon on mRNAs is essential for protein synthesis, which requires scanning and involves eukaryotic initiation factors (eIFs) eIF1, eIF1A, eIF2, and eIF5. The carboxyl terminal domain (CTD) of eIF5 stimulates 43S preinitiation complex (PIC) assembly; however, its precise role in scanning and start codon selection has remained unknown. Using nuclear magnetic resona...

Journal: :Journal of Korean Institute of Fire Science and Engineering 2012

Journal: :Molecular cell 1998
M Muckenthaler N K Gray M W Hentze

Binding of iron regulatory proteins (IRPs) to IREs located in proximity to the cap structure of ferritin H- and L-chain mRNAs blocks ferritin synthesis by preventing the recruitment of the small ribosomal subunit to the mRNA. We have devised a novel procedure to examine the assembly of translation initiation factors (eIFs) on regulated mRNAs. Unexpectedly, we find that the cap binding complex e...

2012
Leoš Shivaya Valášek

Protein synthesis is a fundamental biological mechanism bringing the DNA-encoded genetic information into life by its translation into molecular effectors - proteins. The initiation phase of translation is one of the key points of gene regulation in eukaryotes, playing a role in processes from neuronal function to development. Indeed, the importance of the study of protein synthesis is increasi...

Journal: :EMBO reports 2004
Tatyana V Pestova Ivan B Lomakin Christopher U T Hellen

The cricket paralysis virus intergenic region internal ribosomal entry site (CrPV IGR IRES) can assemble translation initiation complexes by binding to 40S subunits without Met-tRNA(Met)(i) and initiation factors (eIFs) and then by joining directly with 60S subunits, yielding elongation-competent 80S ribosomes. Here, we report that eIF1, eIF1A and eIF3 do not significantly influence IRES/40S su...

Journal: :Cell 2007
Andrey V. Pisarev Christopher U.T. Hellen Tatyana V. Pestova

After translational termination, mRNA and P site deacylated tRNA remain associated with ribosomes in posttermination complexes (post-TCs), which must therefore be recycled by releasing mRNA and deacylated tRNA and by dissociating ribosomes into subunits. Recycling of bacterial post-TCs requires elongation factor EF-G and a ribosome recycling factor RRF. Eukaryotes do not encode a RRF homolog, a...

Journal: :The Biochemical journal 2011
Mark Willett Michele Brocard Alexandre Davide Simon J Morley

Cell migration is a highly controlled essential cellular process, often dysregulated in tumour cells, dynamically controlled by the architecture of the cell. Studies involving cellular fractionation and microarray profiling have previously identified functionally distinct mRNA populations specific to cellular organelles and architectural compartments. However, the interaction between the transl...

Journal: :Journal of molecular biology 2006
Zhiyi Wei Yanyan Xue Hang Xu Weimin Gong

eIF5, a GTPase-activating protein (GAP) specific for eIF2, plays a critical role in pre-initiation complex assembly and correct AUG selection during eukaryotic translation initiation. eIF5 is involved in the formation of the multifactor complex (MFC), an important intermediate of the 43S pre-initiation complex. The C-terminal domain (CTD) of eIF5 functions as the structural core in the MFC asse...

Journal: :Journal of Korean Institute of Fire Science and Engineering 2013

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