Structural highlights
Function
[SYY_METJA] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).[1]
Publication Abstract from PubMed
Marine mussels exhibit potent underwater adhesion abilities under hostile conditions by employing 3,4-dihydroxyphenylalanine (DOPA)-rich mussel adhesive proteins (MAPs). However, their recombinant production is a major biotechnological challenge. Herein, a novel strategy based on genetic code expansion has been developed by engineering efficient aminoacyl-transfer RNA synthetases (aaRSs) for the photocaged noncanonical amino acid ortho-nitrobenzyl DOPA (ONB-DOPA). The engineered ONB-DOPARS enables in vivo production of MAP type 5 site-specifically equipped with multiple instances of ONB-DOPA to yield photocaged, spatiotemporally controlled underwater adhesives. Upon exposure to UV light, these proteins feature elevated wet adhesion properties. This concept offers new perspectives for the production of recombinant bioadhesives.
Photoactivatable Mussel-Based Underwater Adhesive Proteins by an Expanded Genetic Code.,Hauf M, Richter F, Schneider T, Faidt T, Martins BM, Baumann T, Durkin P, Dobbek H, Jacobs K, Moglich A, Budisa N Chembiochem. 2017 Jun 26. doi: 10.1002/cbic.201700327. PMID:28650092[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Steer BA, Schimmel P. Major anticodon-binding region missing from an archaebacterial tRNA synthetase. J Biol Chem. 1999 Dec 10;274(50):35601-6. PMID:10585437
- ↑ Hauf M, Richter F, Schneider T, Faidt T, Martins BM, Baumann T, Durkin P, Dobbek H, Jacobs K, Moglich A, Budisa N. Photoactivatable Mussel-Based Underwater Adhesive Proteins by an Expanded Genetic Code. Chembiochem. 2017 Jun 26. doi: 10.1002/cbic.201700327. PMID:28650092 doi:http://dx.doi.org/10.1002/cbic.201700327
