Results 41 to 50 of about 1,475 (148)

Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation [PDF]

Proceedings of the National Academy of Sciences, 2007
Pyrrolysine (Pyl), the 22nd natural amino acid and genetically encoded by UAG, becomes attached to its cognate tRNA by pyrrolysyl-tRNA synthetase (PylRS). We have determined three crystal structures of the Methanosarcina mazei PylRS complexed with either AMP–PNP, Pyl–AMP plus pyrophosphate, or the Pyl analogue
Jennifer M, Kavran, Sarath, Gundllapalli, Patrick, O'Donoghue, Markus, Englert, Dieter, Söll, Thomas A, Steitz   +5 more
openaire   +2 more sources

Genetic Encoding of Pentafluorophosphato-Phenylalanine Provides PF₅-Proteins as Phosphoprotein Mimetics. [PDF]

Angew Chem Int Ed Engl
Genetic code expansion with a unique hyper‐fluorinated phosphotyrosine analog. In this work, we successfully incorporated the unnatural amino acid pentafluorophosphato‐difluoromethyl‐phenylalanine, carrying seven fluorine atoms and a permanent negative charge into three different proteins via the use of mutated orthogonal aminoacyl‐tRNA synthetases ...
Ambros AM, Qianzhu H, Tiemann M, Habel E, Denzinger K, Zupan H, Accorsi M, Keller BG, Wolber G, Huber T, Rademann J.   +10 more
europepmc   +2 more sources

Molecular Evolution of Aminoacyl tRNA Synthetase Proteins in the Early History of Life [PDF]

, 2011
Aminoacyl-tRNA synthetases (aaRS) consist of several families of functionally conserved proteins essential for translation and protein synthesis. Like nearly all components of the translation machinery, most aaRS families are universally distributed ...
A Suzuki, Cheryl P. Andam, CP Andam, CP Andam, CP Andam, CR Woese, D Korencic, EB Newman, Eric J. Alm, G Srinivasan, GM Nagel, GP Fournier, Gregory P. Fournier, H Grosjean, HS Kim, J Dutheil, J. Peter Gogarten, JA Krzycki, JD Fischer, JF Xiao, JP Gogarten, M Ibba, M Wirtz, O Zhaxybayeva, P Schimmel, RC Edgar, RD Knight, RH White, S Bilokapic, S Cusack, S Fukai, S Guindon, SA Benner, T Suzuki, V Hanson-Smith, Y Ikeuchi, YI Wolf, Z Yang   +37 more
core   +1 more source

Sense codon emancipation for proteome-wide incorporation of noncanonical amino acids : Rare isoleucine codon AUA as a target for genetic code expansion [PDF]

, 2014
One of the major challenges in contemporary synthetic biology is to find a route to engineer synthetic organisms with altered chemical constitution. In terms of core reaction types, nature uses an astonishingly limited repertoire of chemistries when ...
Bohlke, Nina, Budisa, Nediljko
core   +1 more source

Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality [PDF]

Nature, 2008
Pyrrolysine (Pyl), the 22nd natural amino acid, is genetically encoded by UAG and inserted into proteins by the unique suppressor tRNA(Pyl) (ref. 1). The Methanosarcinaceae produce Pyl and express Pyl-containing methyltransferases that allow growth on methylamines.
Nozawa, Kayo, O’Donoghue, Patrick, Gundllapalli, Sarath, Araiso, Yuhei, Ishitani, Ryuichiro, Umehara, Takuya, Soll, Dieter, Nureki, Osamu   +7 more
openaire   +2 more sources

Genetically directed production of recombinant, isosteric and non-hydrolyzable ubiquitin conjugates [PDF]

, 2016
We describe the genetically directed incorporation of aminooxy functionality into recombinant proteins by using a mutant Methanosarcina barkeri pyrrolysyl‐tRNA synthetase/tRNA(CUA) pair.
Adams, Bett, Blight, Carrico, Castañeda, Chen, Chodera, Dirksen, Eger, Emsley, Flierman, Gautier, Haj-Yahya, Haj-Yahya, Hao, Hassiepen, Hemantha, Hershko, Hershko, Jencks, Kabsch, Komander, Komander, Lang, Lewis, Mancini, Matsumoto, Mevissen, Moyal, Nanduri, Nathan, Neumann, Newton, Nguyen, Nguyen, Pal, Popovic, Rabuka, Sato, Schmidt, Schmidt, Schneider, Shanmugham, Sims, Sommer, Sowa, Srinivasan, Tatham, Trang, Ulrich, van der Veen, Virdee, Virdee, Weikart, Wilkinson, Yanagisawa, Ye, Yin, Zhang   +58 more
core   +2 more sources

Rapid Identification of Functional Pyrrolysyl-tRNA Synthetases via Fluorescence-Activated Cell Sorting [PDF]

International Journal of Molecular Sciences, 2018
The orthogonal pyrrolysyl-tRNA synthetase/tRNACUA pair and their variants have provided powerful tools for expanding the genetic code to allow for engineering of proteins with augmented structure and function not present in Nature. To expedite the discovery of novel pyrrolysyl-tRNA synthetase (PylRS) variants that can charge non-natural amino acids ...
Lin, Andrew E., Lin, Qing
openaire   +2 more sources

Aminoacylation of tRNA 2′‐ or 3′‐hydroxyl by phosphoseryl‐ and pyrrolysyl‐tRNA synthetases [PDF]

FEBS Letters, 2013
Class I and II aminoacyl‐tRNA synthetases (AARSs) attach amino acids to the 2′‐ and 3′‐OH of the tRNA terminal adenosine, respectively. One exception is phenylalanyl‐tRNA synthetase (PheRS), which belongs to Class II but attaches phenylalanine to the 2′‐OH.
Englert, Markus, Moses, Sarath, Hohn, Michael, Ling, Jiqiang, O’Donoghue, Patrick, Söll, Dieter   +5 more
openaire   +2 more sources

Site-directed labelling of proteins for NMR and EPR studies [PDF]

, 2018
Site-specific protein labelling presents an important tool for protein structural biology by spectroscopic techniques. This thesis focuses on the development of new spectroscopic labels and labelling strategies to improve the ...
Welegedara, Adarshi Priyanga
core   +1 more source

Optimized Directed Evolution of E. coli leucyl-tRNA Synthetase adds many Noncanonical Amino Acids into the Eukaryotic Genetic Code Including Ornithine and N^ϵ-Acetyl-Methyllysine. [PDF]

Angew Chem Int Ed Engl
The pyrrolysyl pair has dominated noncanonical amino acids (ncAAs) incorporation in eukaryotes, but additional engineerable pairs are needed to further expand this toolbox. Although E. coli leucyl‐tRNA synthetase (EcLeuRS) is a promising candidate, engineering its substrate specificity has been much less successful.
Ficaretta ED, Yared TJ, Bhattacharjee S, Voss LA, Huang RL, Chatterjee A.   +5 more
europepmc   +2 more sources