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At least 667 records · Page 37Linked to original sources
PubMed1986

RNA structural elements for expression in Escherichia coli. Alpha 1-antitrypsin synthesis using translation control elements based on the cII ribosome-binding site of phage lambda.

Analysis of a series of lambda cII::alpha 1-antitrypsin (alpha 1AT) gene fusions of different sizes showed that increased alpha 1AT expression correlated with the stabilisation of a particular computer-predicted RNA secondary structure. Moreover, significant synthesis of unfused alpha 1AT was achieved by reconstruction of this conformation to permit interaction between the upstream region of the ribosome-binding site and the first part of the alpha 1AT coding sequence. This high-level expression was dependent upon certain silent point mutations in the coding sequence, indicating that RNA primary and secondary structure determinants can operate in concert to dictate the efficiency of protein synthesis.

Bacteriophage lambda↗
PubMed1988

Dominance in lambda S mutations and evidence for translational control.

Phenotypic analysis of a collection of point mutations in the lysis gene S of bacteriophage lambda indicates that many of the S alleles exhibit at least partially dominant character, suggesting that the S gene product (gpS) must oligomerize to achieve its lethal membrane effect. Moreover, mutations found 5' to the coding sequence also show a dominant character and appear to define a site, designated sdi (structure directed initiation) where mRNA secondary structure controls the choice of initiation codons. We propose that formation of the sdi structure occludes the consensus Shine-Dalgarno sequence and results in initiation at the Met3 codon, generating a lethal 105 residue polypeptide. The model predicts that, in the absence of the sdi stem-and-loop, initiation occurs at the Met1 codon, generating a 107 residue polypeptide, which is a non-lethal inhibitor of lysis. In support of the model, alteration of the first codon was achieved using site-directed mutagenesis, resulting in an S allele that is more lethal and induces lysis significantly sooner than the wild-type.

Amino Acid Sequence↗