Hfq Lsm family RNA–protein interactions SmAP quaternary structure ribosome biogenesis. In this review, we discuss the structural features of the Lsm family proteins from different life domains and their structure-function relationships. Lsm archaeal proteins (SmAPs) form homoheptamers and likely interact with single-stranded uridine-rich RNA elements, although the role of these proteins in archaea is still poorly understood. Furthermore, recently obtained data indicate a new role of Hfq as a ribosome biogenesis factor, as it mediates formation of the productive structure of the 17S rRNA 3'- and 5'-sequences, facilitating their further processing by RNases. Increase your productivity with AI Sample Finder. Push super-resolution and speed with Airyscan 2. Improve any confocal experiment with LSM Plus. Get high-end confocal imaging in a small footprint. Homohexameric bacterial Lsm protein, Hfq, is involved in the regulation of transcription of different mRNAs by facilitating their interactions with small regulatory RNAs. LSM 900, your compact confocal microscope, provides this with components optimized to deliver the best imaging results. Heteroheptameric eukaryotic Sm and Lsm proteins participate in the formation of spliceosomes and mRNA decapping. A common structural feature of all Lsm family proteins is the presence of the Sm fold consisting of a five-stranded β-sheet and an α-helix at the N-terminus. They are involved in numerous processes associated with RNA processing and gene expression regulation. Members of the Lsm protein family are found in all three domains of life: bacteria, archaea, and eukarya.
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