Translation factor accelerating peptide bond formation on the ribosome: EF-P and eIF5A as entropic catalysts and a potential drug targets

Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers

“…289 This stabilization position forces the nascent peptide chain to adopt an alternative conformation, placing the peptidyl-tRNA into a favorable position for peptidyl transfer. 279,289 As an additional effect of increased polymerization kinetics, EF-P alleviates peptidyl-tRNA dropoff caused by EF-G-driven mistranslocation, decreasing unwanted translation byproducts. 274 While EF-Tu has affinity for all elongator tRNAs and its cognate esterified pAA, E. coli EF-P recognizes only the unique D arm of tRNA Pro isoacceptors and initiator tRNA fMet (Figure 11b, d).…”

“… Often, Lys34 is post-translationally modified to N ε -( R )-β-lysyl- l -hydroxylysine, such as in E. coli , though other modifications include 5-amino­pen­tan­olyl­ation of Lys or rhamnosylation of an analogous Arg residue. − Recently, it was confirmed that Actinobacteria EF-P contain unmodified Lys and instead rely on a more rigid loop sequence . Regardless, this lysine or arginine residue extends into a space adjacent to the CCA-3′ end of the peptidyl-tRNA and forms hydrogen bonds with both rRNA and the peptidyl-tRNA . This stabilization position forces the nascent peptide chain to adopt an alternative conformation, placing the peptidyl-tRNA into a favorable position for peptidyl transfer. , As an additional effect of increased polymerization kinetics, EF-P alleviates peptidyl-tRNA drop-off caused by EF-G-driven mistranslocation, decreasing unwanted translation byproducts …”

“…Regardless, this lysine or arginine residue extends into a space adjacent to the CCA-3′ end of the peptidyl-tRNA and forms hydrogen bonds with both rRNA and the peptidyl-tRNA . This stabilization position forces the nascent peptide chain to adopt an alternative conformation, placing the peptidyl-tRNA into a favorable position for peptidyl transfer. , As an additional effect of increased polymerization kinetics, EF-P alleviates peptidyl-tRNA drop-off caused by EF-G-driven mistranslocation, decreasing unwanted translation byproducts …”

The Structural and Molecular Mechanisms of Mycobacterium tuberculosis Translational Elongation Factor Proteins

“…One important reason for this is the presence of proline residues on the nascent peptide chain. Proline forms proteins more slowly than other amino acids, and tripeptides containing two consecutive prolines are the shortest and most common sequence leading to ribosomal stalling [36]. To address this, the bacterial translation elongation factor P (EF-P) relieves this stalling and allows protein biosynthesis to continue [37].…”

Ukrainian science in the context of its anticolonial struggle

“…Included among the authors are recipients of various prestigious international awards, including the Gregorio Weber Award in Biological Fluorescence and the Hans Neurath Award in Protein Science. The submissions cover a wide area of subjects, ranging from regulation of translation [ 3 , 4 ] and gene activation [5] to protein-membrane interactions [ 6 , 7 ] and cellular signaling [ 2 , [8] , [9] , [10] , [11] ]; from biotechnology [ 12 , 13 ]to structure-function studies of proteins [14] , [15] , [16] , nucleic acids [17] carbohydrates [18] and phosphoglycolipids [19] . The contributions to this issue also cover a broad spectrum of experimental and theoretical approaches, including photochemistry and biochemistry of proton transfer reactions [ 20 , 21 ], quantum chemical modeling [17] and theoretical and experimental exploration of complex spectroscopic responses of amyloids [6] .…”