Hfq Lsm family RNA–protein interactions SmAP quaternary structure ribosome biogenesis. This redirect does not require a rating on the. If you would like to participate, please visit the project page, where you can join the discussion and see a list of open tasks. In this review, we discuss the structural features of the Lsm family proteins from different life domains and their structure-function relationships. This redirect is within the scope of WikiProject Pornography, a collaborative effort to improve the coverage of pornography -related topics on Wikipedia. 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. Homohexameric bacterial Lsm protein, Hfq, is involved in the regulation of transcription of different mRNAs by facilitating their interactions with small regulatory RNAs. 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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