Abstract
We replaced an essential RNA-binding, 30-amino acid helix-loop in an Escherichia coli tRNA synthetase with an inactive and simplified "generic" sequence having 23 of the 30 amino acids as alanine and serine. Wild-type residues were restored in random combinations to generate a library with a sequence complexity of about 1.9 × 107. Active molecules were obtained by genetic selection at a frequency of ≈1% and contained variants with as many as 11 alanine/serine replacements and a total of 17 alanine/serine residues. These variants have activities which are thermodynamically competitive with that of the native protein and therefore are functionally and, most likely, conformationally equivalent.
| Original language | English |
|---|---|
| Pages (from-to) | 10046-10050 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 90 |
| Issue number | 21 |
| DOIs | |
| Publication status | Published - 1993 Nov 1 |
All Science Journal Classification (ASJC) codes
- General
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Kim, S., De Pouplana, L. R., & Schimmel, P. (1993). Diversified sequences of peptide epitope for same-RNA recognition. Proceedings of the National Academy of Sciences of the United States of America, 90(21), 10046-10050. https://doi.org/10.1073/pnas.90.21.10046