Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation

Standard

Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation. / Hountondji, Codjo; Créchet, Jean Bernard; Tanaka, Mayo и др.

в: Biochimie, Том 158, 03.2019, стр. 20-33.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Hountondji, C, Créchet, JB, Tanaka, M, Suzuki, M, Nakayama, JI, Aguida, B, Bulygin, K, Cognet, J, Karpova, G & Baouz, S 2019, 'Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation', Biochimie, Том. 158, стр. 20-33. https://doi.org/10.1016/j.biochi.2018.12.005

APA

Hountondji, C., Créchet, J. B., Tanaka, M., Suzuki, M., Nakayama, J. I., Aguida, B., Bulygin, K., Cognet, J., Karpova, G., & Baouz, S. (2019). Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation. Biochimie, 158, 20-33. https://doi.org/10.1016/j.biochi.2018.12.005

Vancouver

Hountondji C, Créchet JB, Tanaka M, Suzuki M, Nakayama JI, Aguida B и др. Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation. Biochimie. 2019 март;158:20-33. doi: 10.1016/j.biochi.2018.12.005

Author

Hountondji, Codjo ; Créchet, Jean Bernard ; Tanaka, Mayo и др. / Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation. в: Biochimie. 2019 ; Том 158. стр. 20-33.

BibTeX

@article{d036bd565dce4e66b23d72a9e46c6785,

title = "Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation",

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.",

keywords = "eL42 protein from human or Schizosaccharomyces pombe, Eukaryal 80S ribosomes, Lys-55 of S. pombe eL42, Mechanism of peptidyl transfer and peptidyl-tRNA hydrolysis by eukaryotic 80S ribosomes, the GGQ motif of eL42, The peptidyl transferase center of 80S ribosomes from eukaryotes, Schizosaccharomyces/chemistry, Mutation, Missense, Peptide Chain Elongation, Translational/physiology, Schizosaccharomyces pombe Proteins/chemistry, Ribosomes/chemistry, Ribosomal Proteins/chemistry, Catalysis, Amino Acid Substitution, CYCLOHEXIMIDE RESISTANCE, GGQ MOTIF, ESCHERICHIA-COLI, PEPTIDE-BOND FORMATION, TRANSFER RNA-SYNTHETASE, RELEASE FACTOR ERF1, TRANSFERASE CENTER, MESSENGER-RNA, STRUCTURAL BASIS, BINDING-SITE",

author = "Codjo Hountondji and Cr{\'e}chet, {Jean Bernard} and Mayo Tanaka and Mieko Suzuki and Nakayama, {Jun ichi} and Blanche Aguida and Konstantin Bulygin and Jean Cognet and Galina Karpova and Soria Baouz",

year = "2019",

month = mar,

doi = "10.1016/j.biochi.2018.12.005",

language = "English",

volume = "158",

pages = "20--33",

journal = "Biochimie",

issn = "0300-9084",

publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation

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

AU - Karpova, Galina

AU - Baouz, Soria

PY - 2019/3

Y1 - 2019/3

N2 - 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.

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.

KW - eL42 protein from human or Schizosaccharomyces pombe

KW - Eukaryal 80S ribosomes

KW - Lys-55 of S. pombe eL42

KW - Mechanism of peptidyl transfer and peptidyl-tRNA hydrolysis by eukaryotic 80S ribosomes

KW - the GGQ motif of eL42

KW - The peptidyl transferase center of 80S ribosomes from eukaryotes

KW - Schizosaccharomyces/chemistry

KW - Mutation, Missense

KW - Peptide Chain Elongation, Translational/physiology

KW - Schizosaccharomyces pombe Proteins/chemistry

KW - Ribosomes/chemistry

KW - Ribosomal Proteins/chemistry

KW - Catalysis

KW - Amino Acid Substitution

KW - CYCLOHEXIMIDE RESISTANCE

KW - GGQ MOTIF

KW - ESCHERICHIA-COLI

KW - PEPTIDE-BOND FORMATION

KW - TRANSFER RNA-SYNTHETASE

KW - RELEASE FACTOR ERF1

KW - TRANSFERASE CENTER

KW - MESSENGER-RNA

KW - STRUCTURAL BASIS

KW - BINDING-SITE

UR - http://www.scopus.com/inward/record.url?scp=85058559263&partnerID=8YFLogxK

U2 - 10.1016/j.biochi.2018.12.005

DO - 10.1016/j.biochi.2018.12.005

M3 - Article

C2 - 30550856

AN - SCOPUS:85058559263

VL - 158

SP - 20

EP - 33

JO - Biochimie

JF - Biochimie

SN - 0300-9084

ER -

ID: 22848698