Analysis of the developing proteome has been complicated by a lack of tools that can be easily employed to label and identify newly synthesized proteins within complex biological mixtures. Here, we demonstrate that the methionine analogs azidohomoalanine and homopropargylglycine can be globally incorporated into the proteome of mice through facile intraperitoneal injections. These analogs contain bio-orthogonal chemical handles to which fluorescent tags can be conjugated to identify newly synthesized proteins. We show these non-canonical amino acids are incorporated into various tissues in juvenile mice and in a concentration dependent manner. Furthermore, administration of these methionine analogs to pregnant dams during a critical stage of murine development, E10.5-12.5 when many tissues are assembling, does not overtly disrupt development as assessed by proteomic analysis and normal parturition and growth of pups. This successful demonstration that non-canonical amino acids can be directly administered in vivo will enable future studies that seek to characterize the murine proteome during growth, disease and repair.
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http://dx.doi.org/10.1038/srep32377 | DOI Listing |
EMBO Rep
January 2025
Department of Oncological Sciences and Tisch Cancer Institute, Icahn School of Medicine at Mount Sinai, New York, NY, 10029, USA.
To directly examine the interplay between mutant p53 or Mdm2 and wild type p53 in gene occupancy and expression, an integrated RNA-seq and ChIP-seq analysis was performed in vivo using isogenically matched mouse strains. Response to radiation was used as an endpoint to place findings in a biologically relevant context. Unexpectedly, mutant p53 and Mdm2 only inhibit a subset of wild type p53-mediated gene expression.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
January 2025
University of Wisconsin Madison, Chemistry, 1101 University Ave, 53706, Madison, UNITED STATES OF AMERICA.
Many applications of enzymes benefit from activity on structurally diverse substrates. Here, we sought to engineer the decarboxylative aldolase UstD to perform a challenging C-C bond forming reaction with ketone electrophiles. The parent enzyme had only low levels of activity, portending multiple rounds of directed evolution and a possibility that mutations may inadvertently increase the specificity of the enzyme for a single model screening substrate.
View Article and Find Full Text PDFInt J Mol Sci
January 2025
Biotechnology Department, Sirius University of Science and Technology, 354349 Sirius, Russia.
In addition to the 20 canonical amino acids encoded in the genetic code, there are two non-canonical ones: selenocysteine and pyrrolysine. The discovery of pyrrolysine synthetases (PylRSs) was a key event in the field of genetic code expansion research. The importance of this discovery is mainly due to the fact that the translation systems involving PylRS, pyrrolysine tRNA (tRNA) and pyrrolysine are orthogonal to the endogenous translation systems of organisms that do not use this amino acid in protein synthesis.
View Article and Find Full Text PDFPlant Cell Rep
January 2025
Key Laboratory of Crop Molecular Improvement, Rice Research Institute, Academy of Agricultural Sciences, Ministry of Education, Southwest University, Chongqing, 400715, China.
We identified a CXCXCPXC motif and 11 CLG genes that regulate epidermal development by interacting with homeodomain leucine-zipper IV family proteins in Arabidopsis. Zinc finger proteins (ZFPs), the key regulators of plant growth and development, can be categorized based on the sequence patterns of zinc finger motifs. Here, by aligning the amino acid sequences of CFL1, AtCFL1, AtCFL2, GIRl, and GIR2, we identified the CXCXCPXC motif in their C-terminus, which differs from all the previously characterized canonical zinc finger motifs.
View Article and Find Full Text PDFPhotosynth Res
January 2025
Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia.
The Orange Carotenoid Protein (OCP) is a unique water-soluble photoactive protein that plays a critical role in regulating the balance between light harvesting and photoprotective responses in cyanobacteria. The challenge in understanding OCP´s photoactivation mechanism stems from the heterogeneity of the initial configurations of its embedded ketocarotenoid, which in the dark-adapted state can form up to two hydrogen bonds to critical amino acids in the protein's C-terminal domain, and the extremely low quantum yield of primary photoproduct formation. While a series of experiments involving point mutations within these contacts helped us to identify these challenges, they did not resolve them.
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