Congeneric bio-adhesive mussel foot proteins designed by modified prolines revealed a chiral bias in unnatural translation
| Autor: | Shannon Moore, Maud Larregola, Nediljko Budisa |
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| Rok vydání: | 2012 |
| Předmět: |
Future studies
Proline Stereochemistry Molecular Sequence Data Biophysics Biology Biochemistry law.invention law Animals Amino Acid Sequence Molecular Biology Mytilus chemistry.chemical_classification Translation (biology) Cell Biology Mussel Ribosomal RNA Recombinant Proteins Amino acid chemistry Transfer RNA Recombinant DNA Proofreading Cell Adhesion Molecules |
| Zdroj: | Biochemical and Biophysical Research Communications. 421:646-650 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2012.04.031 |
| Popis: | Chiral bias in the unnatural translation and ‘sticky’ mussel proteins. The residue-specific in vivo incorporation of hydroxylated amino acids as well as other synthetic analogs, such as fluoroprolines, emerges as the method of choice for recombinant synthesis of Pro-rich mussel adhesive protein congeners. Chemical diversifications introduced in this way provide a general route towards bio-adhesive congeners endowed with properties not developed by natural evolution. Most importantly, we have found that the co-translational incorporation of (4 R )-, and (4 S )-hyroxylated and fluorinated analogs into mussel proteins presented a chiral bias: the expressed protein was only detectable in samples incubated with analogs with (4 R )-substituents. Possible relationship of these stereochemical preferences for (4 R )-stereoisomers in the translation to intracellular tRNA concentrations, ribosomal editing and proofreading or structural effects such as preorganization remains to be addressed in future studies. These studies will generally provide a mechanistic framework for the flexibility of the translational machinery and establish the boundaries of the unnatural translation. |
| Databáze: | OpenAIRE |
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