article · 19/12/2018
Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation
Résumé
The GGQ minidomain of the ribosomal protein eL42 was previously shown to contact the CCA-arm of P-site bound tRNA in human ribosome, indicating a possible involvement of the protein in the catalytic activity. Here, using Schizosaccharomyces pombe (S. pombe) cells, we demonstrate that the GGQ minidomain and neighboring region of eL42 is critical for the ribosomal function. Mutant eL42 proteins containing amino acid substitutions within or adjacent to the GGQ minidomain failed to complement the function of wild-type eL42, and expression of the mutant eL42 proteins led to severe growth defects. These results suggest that the mutations in eL42 interfere with the ribosomal function in vivo. Furthermore, we show that some of the mutations associated with the conserved GGQ region lead to reduced activities in the poly(Phe) synthesis and/or in the peptidyl transferase reaction with respect to puromycin, as compared with those of the wild-type ribosomes. A pK value of 6.95 was measured for the side chain of Lys-55/Arg-55, which is considerably less than that of a Lys or Arg residue. Altogether, our findings suggest that eL42 contributes to the 80S ribosome's peptidyl transferase activity by promoting the course of the elongation cycle.
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Hountondji, C., Créchet, J.-B., Tanaka, M., Suzuki, M., Nakayama, J.-I., Aguida, B., Bulygin, K., Cognet, J.-A.-H., Karpova, G., & Baouz, S. (2018). Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation. Biochimie, 158(March 2019), 20-33. https://doi.org///doi.org/10.1016/j.biochi.2018.12.005@article{Hountondji2018_305,
author = {Hountondji, Codjo and Créchet, Jean-Bernard and Tanaka, Mayo and Suzuki, Mieko and Nakayama, Jun-Ichi and Aguida, Blanche and Bulygin, Konstantin and Cognet, Jean A. H. and Karpova, Galina and Baouz, Soria},
year = {2018},
month = {12},
title = {Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation},
journal = {Biochimie},
volume = {158},
number = {March 2019},
pages = {20-33},
abstract = {The GGQ minidomain of the ribosomal protein eL42 was previously shown to contact the CCA-arm of P-site bound tRNA in human ribosome, indicating a possible involvement of the protein in the catalytic activity. Here, using Schizosaccharomyces pombe (S. pombe) cells, we demonstrate that the GGQ minidomain and neighboring region of eL42 is critical for the ribosomal function. Mutant eL42 proteins containing amino acid substitutions within or adjacent to the GGQ minidomain failed to complement the function of wild-type eL42, and expression of the mutant eL42 proteins led to severe growth defects. These results suggest that the mutations in eL42 interfere with the ribosomal function in vivo. Furthermore, we show that some of the mutations associated with the conserved GGQ region lead to reduced activities in the poly(Phe) synthesis and/or in the peptidyl transferase reaction with respect to puromycin, as compared with those of the wild-type ribosomes. A pK value of 6.95 was measured for the side chain of Lys-55/Arg-55, which is considerably less than that of a Lys or Arg residue. Altogether, our findings suggest that eL42 contributes to the 80S ribosome's peptidyl transferase activity by promoting the course of the elongation cycle.},
url = {https://www.sciencedirect.com/science/article/pii/S030090841830350X?dgcid=coauthor\#mmc1},
doi = {//doi.org/10.1016/j.biochi.2018.12.005},
}TY - JOUR
AU - Hountondji, Codjo
AU - Créchet, Jean-Bernard
AU - Tanaka, Mayo
AU - Suzuki, Mieko
AU - Nakayama, Jun-Ichi
AU - Aguida, Blanche
AU - Bulygin, Konstantin
AU - Cognet, Jean A. H.
AU - Karpova, Galina
AU - Baouz, Soria
PY - 2018
DA - 2018/12/19
TI - Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation
JO - Biochimie
VL - 158
IS - March 2019
AB - The GGQ minidomain of the ribosomal protein eL42 was previously shown to contact the CCA-arm of P-site bound tRNA in human ribosome, indicating a possible involvement of the protein in the catalytic activity. Here, using Schizosaccharomyces pombe (S. pombe) cells, we demonstrate that the GGQ minidomain and neighboring region of eL42 is critical for the ribosomal function. Mutant eL42 proteins containing amino acid substitutions within or adjacent to the GGQ minidomain failed to complement the function of wild-type eL42, and expression of the mutant eL42 proteins led to severe growth defects. These results suggest that the mutations in eL42 interfere with the ribosomal function in vivo. Furthermore, we show that some of the mutations associated with the conserved GGQ region lead to reduced activities in the poly(Phe) synthesis and/or in the peptidyl transferase reaction with respect to puromycin, as compared with those of the wild-type ribosomes. A pK value of 6.95 was measured for the side chain of Lys-55/Arg-55, which is considerably less than that of a Lys or Arg residue. Altogether, our findings suggest that eL42 contributes to the 80S ribosome's peptidyl transferase activity by promoting the course of the elongation cycle.
SP - 20
EP - 33
DO - //doi.org/10.1016/j.biochi.2018.12.005
UR - https://www.sciencedirect.com/science/article/pii/S030090841830350X?dgcid=coauthor#mmc1
ER -