Sm-like (Lsm) proteins are found in all three domains of life. They are crucially involved in the RNA metabolism of prokaryotic organisms. To exert their function, they assemble into hexa- or heptameric rings and bind RNA via a conserved binding pocket for uridine stretches in the inner pore of the ring. Despite the conserved secondary structure of Lsm proteins, there are several features that lead to a structural diversification of this protein family that mediates their participation in a variety of processes related to RNA metabolism. Until recently, the cellular function of archaeal Sm-like proteins was not well understood. In this review, we discuss structural features of Lsm proteins with a strong focus on archaeal variants, reflect on the evolutionary development of archaeal Lsm proteins and present recent insights into their biological function.
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Cover Image
Cover Image
In the cover image, which depicts archaeal cell division, fl uorescence microscopy shows FtsZ1-GFP localisation in pleomorphic cells of Haloferax volcanii. This archaeal model organism was originally isolated from the Dead Sea, but is well suited to live-cell studies owing to its relatively large, flat cells that show distinct differentiation. Multiple proteins from the tubulin superfamily control cell division and cell shape in this species (see article by Liao et al in this issue; pages 547–559). Archaea are expected to provide important insights into cellular evolution and fundamental cell structures such as the cytoskeleton. Image kindly provided by Iain Duggin (The ithree institute, University of Technology Sydney).
A journey through the evolutionary diversification of archaeal Lsm and Hfq proteins*
Nicholas P. Robinson, Robert Reichelt, Dina Grohmann, Sarah Willkomm; A journey through the evolutionary diversification of archaeal Lsm and Hfq proteins. Emerg Top Life Sci 14 December 2018; 2 (4): 647–657. doi: https://doi.org/10.1042/ETLS20180034
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