Results 31 to 40 of about 1,475 (148)

Pyrrolysine analogues as substrates for pyrrolysyl‐tRNA synthetase [PDF]

FEBS Letters, 2006
In certain methanogenic archaea a new amino acid, pyrrolysine (Pyl), is inserted at in‐frame UAG codons in the mRNAs of some methyltransferases. Pyl is directly acylated onto a suppressor tRNAPyl by pyrrolysyl‐tRNA synthetase (PylRS). Due to the lack of a readily available Pyl source, we looked for structural analogues that could be aminoacylated by ...
Polycarpo, Carla R., Herring, Stephanie, Bérubé, Amélie, Wood, John L., Söll, Dieter, Ambrogelly, Alexandre   +5 more
openaire   +2 more sources

Synthesis of non-linear protein dimers through a genetically encoded thiol-ene reaction [PDF]

, 2014
Site-specific incorporation of bioorthogonal unnatural amino acids into proteins provides a useful tool for the installation of specific functionalities that will allow for the labeling of proteins with virtually any probe.
Chou, C, Deiters, A, Liu, J, Torres-Kolbus, J   +3 more
core   +7 more sources

Recognition of pyrrolysine tRNA by the Desulfitobacterium hafniense pyrrolysyl-tRNA synthetase [PDF]

Nucleic Acids Research, 2007
Pyrrolysine (Pyl), the 22nd co-translationally inserted amino acid, is incorporated in response to a UAG amber stop codon. Pyrrolysyl-tRNA synthetase (PylRS) attaches Pyl to its cognate tRNA, the special amber suppressor tRNA(Pyl). The genes for tRNA(Pyl) (pylT) and PylRS (pylS) are found in all members of the archaeal family Methanosarcinaceae, and in
Herring, Stephanie, Ambrogelly, Alexandre, Polycarpo, Carla R., Söll, Dieter   +3 more
openaire   +2 more sources

Selenocysteine, pyrrolysine and the unique energy metabolism of methanogenic archaea [PDF]

, 2010
Methanogenic archaea are a group of strictly anaerobic microorganisms characterized by their strict dependence on the process of methanogenesis for energy conservation.
Rother, Michael, Krzycki, Joseph A.
core   +1 more source

Expanding the Genetic Code of and to Incorporate Non-canonical Amino Acids for Production of Modified Lantibiotics [PDF]

, 2018
The incorporation of non-canonical amino acids (ncAAs) into ribosomally synthesized and post-translationally modified peptides, e.g., nisin from the Gram-positive bacterium Lactococcus lactis, bears great potential to expand the chemical space of various
Bartholomae, Maike, Baumann, Tobias, Budisa, Nediljko, Kuipers, Oscar P, Nickling, Jessica H, Peterhoff, David, Wagner, Ralf   +6 more
core   +3 more sources

Enhanced incorporation of subnanometer tags into cellular proteins for fluorescence nanoscopy via optimized genetic code expansion [PDF]

, 2022
With few-nanometer resolution recently achieved by a new generation of fluorescence nanoscopes (MINFLUX and MINSTED), the size of the tags used to label proteins will increasingly limit the ability to dissect nanoscopic biological structures ...
Bäte, C., Hell, S., Keller-Findeisen, J., Mihaila, T., Ostersehlt, L., Pape, J., Sahl, S.   +6 more
core   +1 more source

Palladium-unleashed proteins: gentle aldehyde decaging for site-selective protein modification [PDF]

, 2018
Protein bioconjugation frequently makes use of aldehydes as reactive handles, with methods for their installation being highly valued. Here a new, powerful strategy to unmask a reactive protein aldehyde is presented.
Brabham, Robin Louis, Spears, Richard James, Walton, Julia, Tyagi, Swati, Lemke, Edward, Fascione, Martin Anthony   +5 more
core   +5 more sources

Ancient horizontal gene transfer and the last common ancestors [PDF]

, 2015
Background The genomic history of prokaryotic organismal lineages is marked by extensive horizontal gene transfer (HGT) between groups of organisms at all taxonomic levels. These HGT events have played an essential role in the origin and distribution of
A Barzel, A Burt, A Hua-Van, A Sauerwald, A Stoltzfus, AM Barbaglia, B Boussau, B Reisinger, C Darwin, Cheryl P Andam, CP Andam, CP Andam, CR Woese, CR Woese, D Darriba, D Williams, DA Benson, DH Rothman, EGJ Danchin, EV Koonin, EV Koonin, EV Koonin, G Borrel, G Borrel, G Eriani, G Srinivasan, GJ Szöllosi, GM Nagel, GP Fournier, GP Fournier, GP Fournier, Gregory P Fournier, H Grosjean, J Peretó, J Thomas, JA Krzycki, JA Krzycki, JAG Ranea, JL Siefert, JM Kavran, Johann Peter Gogarten, JP Gogarten, K Swithers, K Vetsigian, L Olendzenski, L Ribas de Pouplana, L Ribas de Pouplana, L Sinzelle, LS Frost, M Ibba, M Khomyakova, M Syvanen, M Wu, MH Mazauric, MV Omelchenko, N Lartillot, N Nameki, O Penn, O Zhaxybayeva, P Kück, P Kück, P O’Donoghue, P O’Donoghue, P Schimmel, R Dawkins, R Jain, RC Edgar, S Bilokapic, S Gould, S Guindon, S Herring, S Herring, S Morris, S Osawa, SQ Le, T Tuller, TJ Treangen, VV Kapitonov, WM Fitch, Y Diaz-Lazcoz, Y Zhang, YI Wolf, Z-P Fang   +82 more
core   +2 more sources

Site-specific incorporation of phosphotyrosine using an expanded genetic code. [PDF]

, 2017
Access to phosphoproteins with stoichiometric and site-specific phosphorylation status is key to understanding the role of protein phosphorylation.
Allison Wong, Bing Yang, C Fan, C Hoppmann, Christian Hoppmann, CS Tan, DB Johnson, DT Rogerson, H-G Chao, HS Park, J Xie, JJ Ottesen, JK Takimoto, JP Oza, Kevan M Shokat, L Wang, Lei Wang, M Jbara, MK Tarrant, NL Pirman, P Blume-Jensen, PV Hornbeck, R Serwa, R Yau, RA Chong, S George, SG Julien, Shuwei Li, SJ Humphrey, SW Santoro, T Hunter, T Wauer, Tony Hunter, VK Lacey, WA Lim, Z Chen, Z Xiang   +36 more
core   +1 more source

Switchable genome editing via genetic code expansion [PDF]

, 2018
Multiple applications of genome editing by CRISPR-Cas9 necessitate stringent regulation and Cas9 variants have accordingly been generated whose activity responds to small ligands, temperature or light.
Asami, Maki, Luk, Louis Y. P., Patel, Sanjay G., Perry, Anthony C. F., Suzuki, Toru, Tsai, Yu-Hsuan   +5 more
core   +2 more sources