Abstract
The structure and the RNA-binding properties of the Lsm protein from Halobacterium salinarum have been determined. A distinctive feature of this protein is the presence of a short L4 loop connecting the β3 and β4 strands. Since bacterial Lsm proteins (also called Hfq proteins) have a short L4 loop and form hexamers, whereas archaeal Lsm proteins (SmAP) have a long L4 loop and form heptamers, it has been suggested that the length of the L4 loop may affect the quaternary structure of Lsm proteins. Moreover, the L4 loop covers the region of SmAP corresponding to one of the RNA-binding sites in Hfq, and thus can affect the RNA-binding properties of the protein. Our results show that the SmAP from H. salinarum forms heptamers and possesses the same RNA-binding properties as homologous proteins with the long L4 loop. Therefore, the length of the L4 does not govern the number of monomers in the protein particles and does not affect the RNA-binding properties of Lsm proteins.
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Abbreviations
- DTT:
-
1,4-dithiothreitol
- Lsm protein:
-
Like Sm protein
- SDS:
-
sodium dodecyl sulfate
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Acknowledgments
The authors are grateful to V. Balobanov for help with measurements, V. V. Vrublevskaya for providing antibodies, and colleagues from the Institute of Biological Instrumentation of the Federal Research Center PSCBR, Russian Academy of Sciences, Pushchino, for providing an opportunity to perform SPR experiments.
Funding
The work was supported by the Russian Foundation for Basic Research (project no. 18-04-00222).
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Fando, M.S., Mikhaylina, A.O., Lekontseva, N.V. et al. Structure and RNA-Binding Properties of Lsm Protein from Halobacterium salinarum. Biochemistry Moscow 86, 833–842 (2021). https://doi.org/10.1134/S000629792107004X
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DOI: https://doi.org/10.1134/S000629792107004X