RNA tertiary interactions or tertiary motifs are conserved structural patterns formed by pairwise interactions between nucleotides. They include base-pairing, base-stacking, and base-phosphate interactions. A-minor motifs are the most common tertiary interactions in the large ribosomal subunit. The A-minor motif is a nucleotide triple in which minor groove edges of an adenine base are inserted into the minor groove of neighboring helices, leading to interaction with a stabilizing base pair. We propose here novel features for identifying and predicting A-minor motifs in a given three-dimensional RNA molecule. By utilizing the features together with machine learning algorithms including random forests and support vector machines, we show experimentally that our approach is capable of predicting A-minor motifs in the given RNA molecule effectively, demonstrating the usefulness of the proposed approach. The techniques developed from this work will be useful for molecular biologists and biochemists to analyze RNA tertiary motifs, specifically A-minor interactions.
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http://dx.doi.org/10.1016/j.compbiolchem.2013.10.004 | DOI Listing |
J Bacteriol
January 2025
Department of Microbiology, Howard Taylor Ricketts Laboratory, The University of Chicago, Chicago, Illinois, USA.
Unlabelled: Bacteria transport proteins across the plasma membrane to assemble their envelope, acquire nutrients, and establish appropriate interactions with their environment. The majority of these proteins are synthesized as precursors with a cleavable N-terminal signal sequence for recognition by the Sec machinery. In , a small subset of secreted precursors carries a YSIRK/GXXS motif.
View Article and Find Full Text PDFACS Chem Biol
January 2025
Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, United States.
OaPAC, the photoactivated adenylyl cyclase from , is composed of a blue light using FAD (BLUF) domain fused to an adenylate cyclase (AC) domain. Since both the BLUF and AC domains are part of the same protein, OaPAC is a model for understanding how the ultrafast modulation of the chromophore binding pocket caused by photoexcitation results in the activation of the output domain on the μs-s time scale. In the present work, we use unnatural amino acid mutagenesis to identify specific sites in the protein that are involved in transducing the signal from the FAD binding site to the ATP binding site.
View Article and Find Full Text PDFIn duplex DNA, A-T and G-C form Watson-Crick base pairs, and Hoogsteen pairing only dominates upon protein binding or DNA damage. Using NMR, we show that an A-T Hoogsteen base pair previously observed in crystal structures of transposon DNA hairpins bound to TnpA protein forms in solution even in the absence of TnpA. This Hoogsteen base pair, located adjacent to a dinucleotide apical loop, exists in dynamic equilibrium with a minor Watson-Crick conformation (population ∼11% and lifetime ∼55 µs).
View Article and Find Full Text PDFJ Extracell Vesicles
November 2024
School of Human Sciences, Cell Communication in Disease Pathology, London Metropolitan University, London, UK.
During cell invasion, large Extracellular Vesicle (lEV) release from host cells was dose-dependently triggered by Trypanosoma cruzi metacyclic trypomastigotes (Mtr). This lEV release was inhibited when IP-mediated Ca exit from the ER and further Ca entry from plasma membrane channels was blocked, but whilst any store-independent Ca entry (SICE) could continue unabated. That lEV release was equally inhibited if all entry from external sources was blocked by chelation of external Ca points to the major contributor to Mtr-triggered host cell lEV release being IP/store-mediated Ca release, SICE playing a minor role.
View Article and Find Full Text PDFPLoS One
November 2024
Institute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Protein glycosylation is a fundamental modification crucial for numerous intra- and extracellular functions in all eukaryotes. The phosphorylated dolichol (Dol-P) is utilized in N-linked protein glycosylation and other glycosylation pathways. Dolichol kinase (DK) plays a key role in catalyzing the phosphorylation of dolichol.
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