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• W1591861570 endingPage "8309" @default.
• W1591861570 startingPage "8304" @default.
• W1591861570 abstract "Abstract We have studied the effects of specific amino acid replacements in EF-Tu upon the protein's interactions with guanine nucleotides and elongation factor Ts (EFTs). We found that alterations at the lysine residue of the Asn-Lys-Cys-Asp sequence, the guanine ring-binding sequence, differentially affect the protein's ability to bind guanine nucleotides. Wild type EF-Tu (Lys-136) binds GDP and GTP much more tightly than do many of the altered proteins. Replacing lysine by arginine lowers the protein's affinity for GDP by about 20-fold relative to the change in its affinity for EF-Ts. Substitutions at residue 136 by glutamine (K136Q) and glutamic acid (K136E) further lower the protein relative affinity for GDP by factors of about 4 and 10, respectively. In contrast, replacement of the residue by isoleucine (K136I) eliminates guanine nucleotide binding as well as EF-Ts binding. Apparently, the distortion of this loop by substitution at residue 136 of a bulky hydrophobic residue can hamper the binding for both substrates or disrupt the folding of the protein. All altered proteins except EF-Tu(K136I) are able to bind tRNA(Phe); however, they require much higher concentrations of GTP than wild type EF-Tu. In minimal media, Escherichia coli cells harboring plasmids encoding EF-Tu(K136E) or EF-Tu(K136Q) suffer growth retardation relative to cells bearing the same plasmid encoding wild type EF-Tu. Co-transformation of these cells with a compatible plasmid bearing the EF-Ts gene reverses this growth problem. The growth retardation effect of some of the altered proteins can be explained by their sequestering EF-Ts. These results indicate that EF-Ts is essential to the growth of E. coli and suggest a technique for studying EF-Ts mutants as well as for identifying other guanine nucleotide exchange enzymes." @default.
• W1591861570 created "2016-06-24" @default.
• W1591861570 creator A5058308706 @default.
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• W1591861570 date "1989-05-01" @default.
• W1591861570 modified "2023-09-30" @default.
• W1591861570 title "Mutagenesis of bacterial elongation factor Tu at lysine 136" @default.
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• W1591861570 doi "https://doi.org/10.1016/s0021-9258(18)83183-0" @default.
• W1591861570 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2498311" @default.
• W1591861570 hasPublicationYear "1989" @default.
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