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Domain I of ribosomal protein L1 is sufficient for specific RNA binding.

Tishchenko S, Nikonova E, Kljashtorny V, Kostareva O, Nevskaya N, Piendl W, Davydova N, Streltsov V, Garber M, Nikonov S
Nucleic Acids Res 35 7389-95 (2007)
Cited: 9 times
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Abstract

Ribosomal protein L1 has a dual function as a ribosomal protein binding 23S rRNA and as a translational repressor binding its mRNA. L1 is a two-domain protein with N- and C-termini located in domain I. Earlier it was shown that L1 interacts with the same targets on both rRNA and mRNA mainly through domain I. We have suggested that domain I is necessary and sufficient for specific RNA-binding by L1. To test this hypothesis, a truncation mutant of L1 from Thermus thermophilus, representing domain I, was constructed by deletion of the central part of the L1 sequence, which corresponds to domain II. It was shown that the isolated domain I forms stable complexes with specific fragments of both rRNA and mRNA. The crystal structure of the isolated domain I was determined and compared with the structure of this domain within the intact protein L1. This comparison revealed a close similarity of both structures. Our results confirm our suggestion that in protein L1 its domain I alone is sufficient for specific RNA binding, whereas domain II stabilizes the L1-rRNA complex.

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  2. Domain I of ribosomal protein L1 is sufficient for specific RNA binding. Tishchenko S, Nikonova E, Kljashtorny V, Kostareva O, Nevskaya N, Piendl W, Davydova N, Streltsov V, Garber M, Nikonov S. Nucleic Acids Res 35 7389-7395 (2007)


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  1. The ribosome as a missing link in prebiotic evolution II: Ribosomes encode ribosomal proteins that bind to common regions of their own mRNAs and rRNAs. Root-Bernstein R, Root-Bernstein M. J Theor Biol 397 115-127 (2016)
  2. Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA. Tishchenko S, Kljashtorny V, Kostareva O, Nevskaya N, Nikulin A, Gulak P, Piendl W, Garber M, Nikonov S. J Mol Biol 383 301-305 (2008)
  3. Protein-RNA affinity of ribosomal protein L1 mutants does not correlate with the number of intermolecular interactions. Tishchenko S, Kostareva O, Gabdulkhakov A, Mikhaylina A, Nikonova E, Nevskaya N, Sarskikh A, Piendl W, Garber M, Nikonov S. Acta Crystallogr D Biol Crystallogr 71 376-386 (2015)
  4. Disruption of shape complementarity in the ribosomal protein L1-RNA contact region does not hinder specific recognition of the RNA target site. Kostareva O, Tishchenko S, Nikonova E, Kljashtorny V, Nevskaya N, Nikulin A, Sycheva A, Moshkovskii S, Piendl W, Garber M, Nikonov S. J Mol Recognit 24 524-532 (2011)
  5. RNA-binding protein RPS7 promotes hepatocellular carcinoma progression via LOXL2-dependent activation of ITGB1/FAK/SRC signaling. Zhou YJ, Yang ML, He X, Gu HY, Ren JH, Cheng ST, Fu Z, Zhang ZZ, Chen J. J Exp Clin Cancer Res 43 45 (2024)
  6. Studying the properties of domain I of the ribosomal protein l1: incorporation into ribosome and regulation of the l1 operon expression. Korepanov AP, Kostareva OS, Bazhenova MV, Bubunenko MG, Garber MB, Tishchenko SV. Protein J 34 103-110 (2015)


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