![]() 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. Hfq Lsm family RNA–protein interactions SmAP quaternary structure ribosome biogenesis. This redirect is within the scope of WikiProject Pornography, a collaborative effort to improve the coverage of pornography -related topics on Wikipedia. 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. 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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