eLife, 2021 The ability to regulate DNA replication initiation in response to changing nutrient conditions is an important feature of most cell types. In bacteria, DNA replication is triggered by the initiator protein DnaA, which has long been suggested to respond ...
Michele Felletti +3 more
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Ribosome crystallography: catalysis and evolution of peptide-bond formation, nascent chain elongation and its co-translational folding [PDF]
Biochemical Society Transactions, 2005 A ribosome is a ribozyme polymerizing amino acids, exploiting positional- and substrate-mediated chemical catalysis. We showed that peptide-bond formation is facilitated by the ribosomal architectural frame, provided by a sizable symmetry-related region in and around the peptidyl transferase centre, suggesting that the ribosomal active site was evolved
A, Bashan, A, Yonath
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Dual regulation of translation initiation and peptide chain elongation during BDNF‐induced LTP in vivo: evidence for compartment‐specific translation control [PDF]
Journal of Neurochemistry, 2006 AbstractProtein synthesis underlying activity‐dependent synaptic plasticity is controlled at the level of mRNA translation. We examined the dynamics and spatial regulation of two key translation factors, eukaryotic initiation factor 4E (eIF4E) and elongation factor‐2 (eEF2), during long‐term potentiation (LTP) induced by local infusion of brain‐derived
Tambudzai, Kanhema +9 more
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SecM-stalled ribosomes adopt an altered geometry at the peptidyl transferase center. [PDF]
PLoS Biology, 2011 As nascent polypeptide chains are synthesized, they pass through a tunnel in the large ribosomal subunit. Interaction between specific nascent chains and the ribosomal tunnel is used to induce translational stalling for the regulation of gene expression.
Shashi Bhushan +7 more
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Co-translational localization of an LTR-retrotransposon RNA to the endoplasmic reticulum nucleates virus-like particle assembly sites. [PDF]
PLoS Genetics, 2014 The transcript of retrovirus-like transposons functions as an mRNA for synthesis of capsid and replication proteins and as the genomic RNA of virus-like particles (VLPs), wherein the genome is replicated.
Jung H Doh, Sheila Lutz, M Joan Curcio
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Extensive evolution of cereal ribosome-inactivating proteins translates into unique structural features, activation mechanisms, and physiological roles [PDF]
, 2017 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
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Active role of elongation factor G in maintaining the mRNA reading frame during translation. [PDF]
, 2019 During translation, the ribosome moves along the mRNA one codon at a time with the help of elongation factor G (EF-G). Spontaneous changes in the translational reading frame are extremely rare, yet how the precise triplet-wise step is maintained is not ...
Belardinelli, R. +5 more
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Cotranslational folding of proteins on the ribosome.
, 2020 Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different ways ...
Liutkute, M., Rodnina, M., Samatova, E.
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An in vivo control map for the eukaryotic mRNA translation machinery [PDF]
, 2013 Rate control analysis defines the in vivo control map governing yeast protein synthesis and generates an extensively parameterized digital model of the translation pathway.
Amy Claydon +12 more
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Revealing nascent proteomics in signaling pathways and cell differentiation. [PDF]
, 2018 Regulation of gene expression at the level of protein synthesis is a crucial element in driving how the genetic landscape is expressed. However, we are still limited in technologies that can quantitatively capture the immediate proteomic changes that ...
Burlingame, Alma L +8 more
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