Interaction between a mutant release factor one and P‐site peptidyl‐tRNA is influenced by the identity of the two bases downstream of the stop codon UAG

FEBS Letters

Rydén-Aulin, Monica¹  Isaksson, Leif A¹  Zhang, Shaoping¹ 

[1] Department of Microbiology, Stockholm University, S-106 91 Stockholm, Sweden

关键词: Translation termination;    Codon context;    P-site tRNA;    Escherichia coli;    RF;    release factor;    EFTu;    elongation factor Tu;    Ts;    temperature sensitive;   

DOI  :  10.1016/S0014-5793(99)00912-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Termination efficiency of a mutant form of RF (release facor) 1, as compared to the wild-type enzyme, is influenced by the P-site peptidyl-tRNA if the termination signal is UAGA. This effect is weaker at the stronger termination signal UAGU. Similarly, low efficiency of the mutant RF1, together with certain peptidyl-tRNAs, can be increased by changing the second base of the 3′-flanking codon from C to G. The data suggest that the mutant RF1 interacts with the P-site peptidyl-tRNA in conjunction with the context at the 3′-side of the termination codon.

【 授权许可】

Unknown