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N Bilgin

Publications and source records attributed to N Bilgin.

At least 145 records · Page 8Linked to original sources

Two GTPs are hydrolysed on two molecules of EF-Tu for each elongation cycle during code translation.

A new experimental design has been used to determine the number of GTPs hydrolysed per peptide bond in EF-Tu function in a poly(U)-translation system. We find that two GTPs are consumed for every amino acid incorporated into the nascent poly(Phe)-chains, in accordance with previous findings with other techniques. These results necessitate a revision of current views concerning E coli translation; also new schemes for ribosome function are discussed.

Buffers↗

Kinetic properties of Escherichia coli ribosomes with altered forms of S12.

E. coli ribosomes with alterations in S12 leading to streptomycin resistance (SmR), dependence (SmD) and pseudodependence (SmP) were studied with the quench-flow technique. Kinetic changes at the various steps of the elongation cycle were identified. The rate of hydrolysis of GTP in the ternary complex in the ribosomal A-site is decreased drastically in SmD and moderately in SmP in relation to wild-type ribosomes. Addition of streptomycin restores much of the wild-type behaviour. The SmD, SmP and SmR ribosomes have an enhanced GTP-hydrolysis idling reaction on EF-Tu, which is correlated with how aggressive proofreaders these ribosomes are in steady-state assays. We use our in vitro findings to discuss the in vivo physiology of these mutants as well as mechanistic features of E. coli translation.

Escherichia coli↗