Abstract
L1 is a conserved protein of the large ribosomal subunit. This protein binds strongly to the specific region of the high molecular weight rRNA of the large ribosomal subunit, thus forming a conserved flexible structural element—the L1 stalk. L1 protein also regulates translation of the operon that comprises its own gene. Crystallographic data suggest that L1 interacts with RNA mainly by means of its domain I. We show here for the first time that the isolated domain I of the bacterial protein L1 of Thermus thermophilus and Escherichia coli is able to incorporate in vivo into the E. coli ribosome. Furthermore, domain I of T. thermophilus L1 can regulate expression of the L1 gene operon of Archaea in the coupled transcription–translation system in vitro, as well as the intact protein. We have identified the structural elements of domain I of the L1 protein that may be responsible for its regulatory properties.
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Abbreviations
- r-protein:
-
Ribosomal protein
- EcoL1:
-
L1 protein of E. coli
- MvaL1:
-
L1 protein of M. vannielii
- TthL1d1:
-
TthL1 domain I
- EcoL1d1:
-
E. coli L1 protein domain I
- ORF:
-
Open reading frame
- H-bonds:
-
Hydrogen bonds
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Acknowledgments
The authors thank Dr. Alexander Kaliman (Institute of Protein Research) and Dr. Donald L. Court (National Cancer Institute at Frederick) for the plasmids provided. This study was supported by the Program “Molecular and cellular biology” of the Presidium of the Russian Academy of Sciences and the Russian Foundation for Basic Research (Grants No. 14-04-00414 and No. 15-04-05008). SPR experiments were performed at the Human Proteome Shared Facility Center of the Institute of Biomedical Chemistry, Moscow, Russia.
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Korepanov, A.P., Kostareva, O.S., Bazhenova, M.V. et al. Studying the Properties of Domain I of the Ribosomal Protein L1: Incorporation into Ribosome and Regulation of the L1 Operon Expression. Protein J 34, 103–110 (2015). https://doi.org/10.1007/s10930-015-9602-5
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DOI: https://doi.org/10.1007/s10930-015-9602-5