Results 111 to 120 of about 12,851,211 (266)

Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic code

eLife, 2014
Aminoacyl-tRNA synthetases use a variety of mechanisms to ensure fidelity of the genetic code and ultimately select the correct amino acids to be used in protein synthesis.
Tammy J Bullwinkle, Noah M Reynolds, Medha Raina, Adil Moghal, Eleftheria Matsa, Andrei Rajkovic, Huseyin Kayadibi, Farbod Fazlollahi, Christopher Ryan, Nathaniel Howitz, Kym F Faull, Beth A Lazazzera, Michael Ibba   +12 more
doaj   +1 more source

In silico and in vitro exploration of a tyrosinase for biocatalytic production of catechols

FEBS Open Bio, EarlyView.
Tyrosinase from Ralstonia pseudosolanacearum is a promising biocatalyst for producing valuable catechols from monophenol substrates. This tyrosinase is uniquely suited to this due to its high monophenolase : diphenolase ratio. We combined in silico docking and in vivo kinetic characterisation of this tyrosinase with 11 industrially relevant monophenols,
James Britton, Fang Zhao, Reeta Davis, Meg Walsh, Kevin E O'Connor, David O'Connell, Tanja Narancic   +6 more
wiley   +1 more source

Purification and preparation of Marchantia polymorpha Auxin Response Factor 2 for phase separation studies

FEBS Open Bio, EarlyView.
We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen, Robin Romein, Willy A. M. van den Berg, Simon Lindhoud, Jan Willem Borst, Carlo P. M. van Mierlo   +5 more
wiley   +1 more source

Expanding the genetic code: phage-driven evolution of pyrrolysyl-synthetase for site-specific incorporation of synthetic phenylalanine and tyrosine derivatives

Frontiers in Molecular Biosciences
IntroductionPyrrolysyl-tRNA synthetase (PylRS) is a key enzyme for the site-specific incorporation of non-canonical amino acids (ncAAs) into proteins. However, its native form has a limited substrate scope.
Anastasia Dakhnevich, Sabina Miasoutova, Danila Iliushin, Aleksey Rozanov, Roman Ivanov   +4 more
doaj   +1 more source

Avidin is evolutionarily conserved in fish but dispensable for development and resistance against Streptococcus agalactiae in zebrafish

FEBS Open Bio, EarlyView.
The presence of biotin‐binding avidin proteins in fish and their biological significance are poorly characterized. We cataloged fish avidins and demonstrate that they are widely present and evolutionarily conserved. We created avd knockout zebrafish and show that zebavidin is dispensable for development and that resistance of avd knockout embryos in ...
Anni K. Saralahti, Markus J. T. Ojanen, Mataleena Parikka, Otto Kauko, Mika Rämet, Vesa P. Hytönen   +5 more
wiley   +1 more source

Enzymes with Non-Canonical Amino Acids

Enzyme design and engineering strategies rely almost exclusively on Nature’s alphabet of twenty canonical amino acids. Recent years have seen the emergence of powerful genetic code expansion methods that allow hundreds of structurally diverse amino acids
Burke, Ashleigh, Green, Anthony; id_orcid, Zhao, Jingming   +2 more
core   +7 more sources

Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum

FEBS Open Bio, EarlyView.
In this study, a novel esterase from the thermoacidophilic archaeon Thermoplasma acidophilum was biochemically and structurally characterized. Our results demonstrate that Ta0887 is a highly thermostable esterase that preferentially hydrolyzes p‐nitrophenyl hexanoate and possesses an α‐helical cap domain that likely contributes to its substrate ...
Alejandro Delgado‐Rey, Miriam Livier Llamas‐García, Gabriela M. Montero‐Morán, Leticia Santos, Samuel Lara‐González   +4 more
wiley   +1 more source

Threonine 348 regulates the subcellular localization of PTEN

FEBS Open Bio, EarlyView.
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley   +1 more source

Genetic dissection of human ABCE1 in yeast reveals separable requirements for ribosome recycling and suppression of aberrant reinitiation

FEBS Open Bio, EarlyView.
Human ABCE1 cannot functionally replace its yeast ortholog. Yeast–human chimera analysis identified NBD1 as a major interspecies barrier. Genetic screening yielded hABCE1 revertants that rescue yeast viability but fail to suppress aberrant translation reinitiation in the 3′ UTR.
Eriko Nakata, Yuxin Li, Kei Endo, Koichi Ito   +3 more
wiley   +1 more source

The invertebrate transporters of SLC6 family are able to transport D-amino acid

, 2017
Neutral amino acids, which predominantly represent essential substrates in animals, are absorbed via a B0 transport system (the Broad neutral amino acid system).
E. Bossi, M. Castagna, A. Vollero, R. Cinquetti   +3 more
core   +2 more sources