Stoichiometry and Change of the mRNA Closed-Loop Factors as Translating Ribosomes Transit from Initiation to Elongation [PDF]
Protein synthesis is a highly efficient process and is under exacting control. Yet, the actual abundance of translation factors present in translating complexes and how these abundances change during the transit of a ribosome across an mRNA remains ...
Chiang, Yueh-Chin +6 more
core +4 more sources
Divergent effects of fluoroaluminates on the peptide chain elongation factors EF‐Tu and EF‐G as members of the GTPase superfamily [PDF]
Fluoroaluminates are thought to mimic the γ‐phosphate of GTP and thus, together with GDP, perturb the functioning of heterotrimeric GTP‐binding G‐proteins. Here we show they do inhibit the ribosome‐stimulated GTPase activity of EF‐G from Escherichia coli via the formation of a stable complex with EF‐G·GDP and ribosomes.
Mesters, Jeroen R. +2 more
openaire +2 more sources
The role of molecular chaperone CCT/TRiC in translation elongation: A literature review
Protein synthesis from mRNA is an energy-intensive and strictly controlled biological process. Translation elongation is a well-coordinated and multifactorial step in translation that ensures the accurate and efficient addition of amino acids to a ...
Yueyue Que +6 more
doaj +1 more source
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes +4 more
wiley +1 more source
IntroductionTranslation is a fundamental process of life. In eukaryotes, the elongation step of translation is highly conserved and is driven by eukaryotic translation elongation factors (eEF)1A and eEF2.
Giovanna Maldonado +7 more
doaj +1 more source
Identification of the prebiotic translation apparatus within the contemporary ribosome [PDF]
A structural element that could have existed independently in the prebiotic era was identified at the active site of the contemporary ribosome. It is suggested to have functioned as a proto-ribosome catalyzing peptide bond formation and non-coded ...
Ada Yonath +3 more
core +1 more source
Template-directed biopolymerization: tape-copying Turing machines
DNA, RNA and proteins are among the most important macromolecules in a living cell. These molecules are polymerized by molecular machines. These natural nano-machines polymerize such macromolecules, adding one monomer at a time, using another linear ...
Chowdhury, Debashish, Sharma, Ajeet K.
core +1 more source
Extensive evolution of cereal ribosome-inactivating proteins translates into unique structural features, activation mechanisms, and physiological roles [PDF]
Ribosome-inactivating proteins (RIPs) are a class of cytotoxic enzymes that can depurinate rRNAs thereby inhibiting protein translation. Although these proteins have also been detected in bacteria, fungi, and even some insects, they are especially ...
De Zaeytijd, Jeroen, Van Damme, Els
core +2 more sources
COMP–PMEPA1 axis promotes epithelial‐to‐mesenchymal transition in breast cancer cells
This study reveals that cartilage oligomeric matrix protein (COMP) promotes epithelial‐to‐mesenchymal transition (EMT) in breast cancer. We identify PMEPA1 (protein TMEPAI) as a novel COMP‐binding partner that mediates EMT via binding to the TSP domains of COMP, establishing the COMP–PMEPA1 axis as a key EMT driver in breast cancer.
Konstantinos S. Papadakos +6 more
wiley +1 more source
Elongation factor 2-diphthamide is critical for translation of two IRES-dependent protein targets, XIAP and FGF2, under oxidative stress conditions [PDF]
Elongation factor-2 (eEF2) catalyzes the movement of the ribosome along the mRNA. A single histidine residue in eEF2 (H715) is modified to form diphthamide. A role for eEF2 in cellular stress responses is highlighted by the fact that eEF2 is sensitive to
Argüelles Castilla, Sandro +3 more
core +1 more source

