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| http://dx.doi.org/10.1002/anie.201302811 | DOI Listing |
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Structural Insights into the Rrp4 Subunit from the Crystal Structure of the Exosome.
Biomolecules
May 2024
Department of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 02841, Republic of Korea.
The exosome multiprotein complex plays a critical role in RNA processing and degradation. This system governs the regulation of mRNA quality, degradation in the cytoplasm, the processing of short noncoding RNA, and the breakdown of RNA fragments. We determined two crystal structures of exosome components from (): one with a resolution of 2.
View Article and Find Full Text PDFThe archaeal Lsm protein from binds co-transcriptionally to poly(U)-rich target RNAs.
Biol Chem
October 2023
Institute of Microbiology & Archaea Centre, Single-Molecule Biochemistry Lab, University of Regensburg, D-93053 Regensburg, Germany.
Posttranscriptional processes in Bacteria include the association of small regulatory RNAs (sRNA) with a target mRNA. The sRNA/mRNA annealing process is often mediated by an RNA chaperone called Hfq. The functional role of bacterial and eukaryotic Lsm proteins is partially understood, whereas knowledge about archaeal Lsm proteins is scarce.
View Article and Find Full Text PDFIsolation, Purification, and Characterization of Membrane Vesicles from Haloarchaea.
Methods Mol Biol
September 2022
Max-Planck Institute for Marine Microbiology, Bremen, Germany.
Membrane vesicles (MVs), also described as extracellular vesicles (EVs), exosomes, or outer membrane vesicles (OMVs), are nano-sized (10-300 nm) spherical, membrane-bound structures deriving from the cell envelope. MVs have been studied extensively in both eukaryotic and prokaryotic systems, revealing a plethora of unique functions including cell-to-cell communication and protection of the cell. They are able to encapsulate specific cargos from nucleic acids to proteins, thereby concentrating cargo and providing protection from the extracellular environment.
View Article and Find Full Text PDFCharacterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex.
Mol Microbiol
July 2022
CNRS, CEA, IBS, Univ Grenoble Alpes, Grenoble, France.
Article Synopsis
- The proteasome system is responsible for degrading damaged or unneeded proteins, including newly formed peptides, but its interaction with translation machinery in Archaea is not well understood.
- Researchers studied a small protein called Q9UZY3, now named Pbp11, which was identified using the proteasome-activating nucleotidase (PAN) as bait in experiments.
- Pbp11 has a unique structure and binds to tRNA, indicating it plays a significant role in connecting the proteasome and translation processes, as it interacts with the proteasome machinery and includes various related proteins in its interaction network.
Morphomolecular Characterization of Serum Nanovesicles From Microbiomes Differentiates Stable and Infarcted Atherosclerotic Patients.
Front Cardiovasc Med
August 2021
Laboratorio de Patologia Cardiaca, Instituto do Coracao, Hospital das Clinicas HCFMUSP, Faculdade de Medicina, Universidade de São Paulo, São Paulo, Brazil.
Microbial communities are considered decisive for maintaining a healthy situation or for determining diseases. Acute myocardial infarction (AMI) is an important complication of atherosclerosis caused by the rupture of atheroma plaques containing proinflammatory cytokines, reactive oxygen species, oxidized low-density lipoproteins (oxLDL), damaged proteins, lipids, and DNA, a microenvironment compatible with a pathogenic microbial community. Previously, we found that archaeal DNA-positive infectious microvesicles (iMVs) were detected in vulnerable plaques and in the sera of Chagas disease patients with heart failure.
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