Mancera-Martínez Eder, Dong Yihan, Makarian Joelle, Srour Ola, Thiébeauld Odon, Jamsheer Muhammed, Chicher Johana, Hammann Philippe, Schepetilnikov Mikhail, Ryabova Lyubov A.
Phosphorylation of a reinitiation supporting protein, RISP, determines its function in translation reinitiation Journal Article
In: Nucleic Acids Research, vol. 49, no. 12, pp. 6908–6924, 2021, ISSN: 1362-4962.
Abstract | Links | BibTeX | Tags: Arabidopsis, Arabidopsis Proteins, Caulimovirus, Eukaryotic, Eukaryotic Initiation Factor-2B, Eukaryotic Initiation Factor-3, Large, Peptide Chain Initiation, Phosphorylation, PPSE, Ribosomal Protein S6, Ribosome Subunits, translational
@article{mancera-martinez_phosphorylation_2021,
title = {Phosphorylation of a reinitiation supporting protein, RISP, determines its function in translation reinitiation},
author = {Eder Mancera-Martínez and Yihan Dong and Joelle Makarian and Ola Srour and Odon Thiébeauld and Muhammed Jamsheer and Johana Chicher and Philippe Hammann and Mikhail Schepetilnikov and Lyubov A. Ryabova},
doi = {10.1093/nar/gkab501},
issn = {1362-4962},
year = {2021},
date = {2021-07-01},
journal = {Nucleic Acids Research},
volume = {49},
number = {12},
pages = {6908--6924},
abstract = {Reinitiation supporting protein, RISP, interacts with 60S (60S ribosomal subunit) and eIF3 (eukaryotic initiation factor 3) in plants. TOR (target-of-rapamycin) mediates RISP phosphorylation at residue Ser267, favoring its binding to eL24 (60S ribosomal protein L24). In a viral context, RISP, when phosphorylated, binds the CaMV transactivator/ viroplasmin, TAV, to assist in an exceptional mechanism of reinitiation after long ORF translation. Moreover, we show here that RISP interacts with eIF2 via eIF2β and TOR downstream target 40S ribosomal protein eS6. A RISP phosphorylation knockout, RISP-S267A, binds preferentially eIF2β, and both form a ternary complex with eIF3a in vitro. Accordingly, transient overexpression in plant protoplasts of RISP-S267A, but not a RISP phosphorylation mimic, RISP-S267D, favors translation initiation. In contrast, RISP-S267D preferentially binds eS6, and, when bound to the C-terminus of eS6, can capture 60S in a highly specific manner in vitro, suggesting that it mediates 60S loading during reinitiation. Indeed, eS6-deficient plants are highly resistant to CaMV due to their reduced reinitiation capacity. Strikingly, an eS6 phosphomimic, when stably expressed in eS6-deficient plants, can fully restore the reinitiation deficiency of these plants in cellular and viral contexts. These results suggest that RISP function in translation (re)initiation is regulated by phosphorylation at Ser267.},
keywords = {Arabidopsis, Arabidopsis Proteins, Caulimovirus, Eukaryotic, Eukaryotic Initiation Factor-2B, Eukaryotic Initiation Factor-3, Large, Peptide Chain Initiation, Phosphorylation, PPSE, Ribosomal Protein S6, Ribosome Subunits, translational},
pubstate = {published},
tppubtype = {article}
}
Benelli D, Marzi S, Mancone C, Alonzi T, la Teana A, Londei P
Function and ribosomal localization of aIF6, a translational regulator shared by archaea and eukarya Journal Article
In: Nucleic Acids Res, vol. 37, no. 1, pp. 256-267, 2009, ISBN: 19036786, (1362-4962 (Electronic) Journal Article Research Support, Non-U.S. Gov't).
Abstract | Links | BibTeX | Tags: 23S/chemistry/metabolism Ribosomal Proteins/metabolism Ribosome Subunits, Archaeal Proteins/analysis/chemistry/*metabolism Base Sequence Binding Sites Cell Cycle Cloning, Archaeal/*metabolism Ribosomes/metabolism Sulfolobus solfataricus/*genetics/metabolism, Large, Molecular Eukaryotic Initiation Factors/chemistry Models, Molecular Molecular Sequence Data Prokaryotic Initiation Factors/analysis/chemistry/*metabolism *Protein Biosynthesis RNA, Ribosomal, ROMBY, Unité ARN
@article{,
title = {Function and ribosomal localization of aIF6, a translational regulator shared by archaea and eukarya},
author = {D Benelli and S Marzi and C Mancone and T Alonzi and A la Teana and P Londei},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19036786},
isbn = {19036786},
year = {2009},
date = {2009-01-01},
journal = {Nucleic Acids Res},
volume = {37},
number = {1},
pages = {256-267},
abstract = {The translation factor IF6 is shared by the Archaea and the Eukarya, but is not found in Bacteria. The properties of eukaryal IF6 (eIF6) have been extensively studied, but remain somewhat elusive. eIF6 behaves as a ribosome-anti-association factor and is involved in miRNA-mediated gene silencing; however, it also seems to participate in ribosome synthesis and export. Here we have determined the function and ribosomal localization of the archaeal (Sulfolobus solfataricus) IF6 homologue (aIF6). We find that aIF6 binds specifically to the 50S ribosomal subunits, hindering the formation of 70S ribosomes and strongly inhibiting translation. aIF6 is uniformly expressed along the cell cycle, but it is upregulated following both cold- and heat shock. The aIF6 ribosomal binding site lies in the middle of the 30-S interacting surface of the 50S subunit, including a number of critical RNA and protein determinants involved in subunit association. The data suggest that the IF6 protein evolved in the archaeal-eukaryal lineage to modulate translational efficiency under unfavourable environmental conditions, perhaps acquiring additional functions during eukaryotic evolution.},
note = {1362-4962 (Electronic)
Journal Article
Research Support, Non-U.S. Gov't},
keywords = {23S/chemistry/metabolism Ribosomal Proteins/metabolism Ribosome Subunits, Archaeal Proteins/analysis/chemistry/*metabolism Base Sequence Binding Sites Cell Cycle Cloning, Archaeal/*metabolism Ribosomes/metabolism Sulfolobus solfataricus/*genetics/metabolism, Large, Molecular Eukaryotic Initiation Factors/chemistry Models, Molecular Molecular Sequence Data Prokaryotic Initiation Factors/analysis/chemistry/*metabolism *Protein Biosynthesis RNA, Ribosomal, ROMBY, Unité ARN},
pubstate = {published},
tppubtype = {article}
}