Physiologically, in normal cells under stimuli such as growth factors and nutrients, the productions of RPs and rRNAs are coordinated to balance for ribosome assembly and translation Warner, , thus maintaining proper cell growth and proliferation.
Once the balance between RPs and rRNAs or the balance among different RPs is lost, ribosome biogenesis may malfunction, and the excess RPs may exert extraribosomal functions, such as induction of ribosomal stress Warner and McIntosh, Through the variation of nucleolar integrity, RPs can be released from nucleolus to nucleoplasm and perform the extraribosomal functions, thus responding to diverse types of cellular stress Rubbi and Milner, Deregulation of RPs, which are caretakers for cellular stress and growth, increases cancer risk and plays important roles in cancer development Goudarzi and Lindstrom, Abnormal expressions or mutations in RP genes are observed in human malignancies de Las Heras-Rubio et al.
However, the identities of regulators and the mechanism for the transition between ribosomal and extraribosomal function of RPs remain largely unclear. BCCIP deficiency causes homologous recombination defects, spontaneous chromatid aberrations, cytokinesis failure, and cell cycle dysregulation Meng et al. Although the two isoforms have much in common in terms of the biochemical characteristics, they perform some preferential functions Meng et al.
Cell lysates were then immunoprecipitated with Flag or Myc antibodies, and the bound proteins were detected by western blotting. The potential protein complex was separated using GST beads and detected by western blotting with Flag antibody. Eukaryote-specific motif of ribosomal protein S15 neighbors A site codon during elongation and termination of translation.
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Russian Journal of Bioorganic Chemistry , 34 6 , Biochimie , 90 , Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes. The C-terminal fragment of ribosomal protein S15 is located in the decoding site of the human ribosome. Molecular Biology , 42 2 , Bulygin, S. Baouz-Drahy, A. Favre, D. Russian Journal of Bioorganic Chemistry , 34 1 , Molotkov, D.
Graifer, E. Popugaeva, K. Bulygin, M. Meschaninova, A. Russian Journal of Bioorganic Chemistry , 33 4 , Laletina, D. Russian Journal of Bioorganic Chemistry , 32 3 , Dubovaya, P. Kolosov, E. Alkalaeva, L. Frolova, L. Influence of individual domains of the translation termination factor eRF1 on induction of the GTPase activity of the translation termination factor eRF3.
Molecular Biology , 40 2 , Eukaryotic ribosomal proteins lacking a eubacterial counterpart: important players in ribosomal function. Molecular Microbiology , 59 6 , Mitkevich, A. Kononenko, N. Oparina, P. Kolosov, A. Makarov, L. Thermal denaturation of class 1 eukaryotic translation termination factor eRF1.
Relationship between stability and functional activity of eRF1 mutants. Molecular Biology , 40 1 , Antoine, K. Reimers, W. Wirz, A.Grosheva, Yulia S. Franckenberg, V. However, the regulations for transition between the ribosomal and extraribosomal functions of RPs are rarely reported. Dmitri Graifer, Galina Karpova. Laletina, D. Khairulina, M. Laletina, D. Becker, S. Biochimie92 7The C-terminal refund of ribosomal protein S15 is bad in the decoding site of the human ribosome. Armache, A. Oparina, P. Marquez, T.
Cited By This article is cited by 23 publications. Meschaninova, A. Biochimie , 90 ,
Molecular Biology , 42 2 ,
Gressner, R. Cited By This article is cited by 23 publications. Jossinet, M. Ven'yaminova, Joachim Stahl, Dmitri M. Russian Journal of Bioorganic Chemistry , 33 4 ,