scholarly journals Ribosomal protein S19-binding domain provides insights into hantavirus nucleocapsid protein-mediated translation initiation mechanism

2014 ◽  
Vol 464 (1) ◽  
pp. 109-121 ◽  
Author(s):  
Safder S. Ganaie ◽  
Absarul Haque ◽  
Erdong Cheng ◽  
Tania S. Bonny ◽  
Nilshad N. Salim ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ribosomal Protein ◽  
Translation Initiation ◽  
Nucleocapsid Protein ◽  
Binding Domain ◽  
Initiation Mechanism ◽  
Translation Initiation Mechanism ◽  
Ribosomal Protein S19

The binding domain for the ribosomal protein S19 was mapped to amino acids 151–175 of hantavirus nucleocapsid protein (N). This study provides insights about the mechanism of ribosome loading during the N-mediated translation initiation strategy.

scholarly journals Interaction of Hantavirus Nucleocapsid Protein with Ribosomal Protein S19

2010 ◽  
Vol 84 (23) ◽  
pp. 12450-12453 ◽  
Author(s):  
Absarul Haque ◽  
Mohammad A. Mir
Keyword(s):  
Ribosomal Protein ◽  
Translation Initiation ◽  
Nucleocapsid Protein ◽  
Ribosomal Proteins ◽  
18S Rrna ◽  
Ribosomal Subunit ◽  
Head Region ◽  
40S Ribosomal Subunit ◽  
Ribosomal Protein S19 ◽  
Viral Nucleocapsid

ABSTRACT Hantaviruses, members of the Bunyaviridae family, are emerging category A pathogens that initiate the translation of their capped mRNAs by a novel mechanism mediated by viral nucleocapsid protein (N). N specifically binds to the mRNA 5′ m7G cap and 40S ribosomal subunit, a complex of 18S rRNA and multiple ribosomal proteins. Here, we show that N specifically interacts with the ribosomal protein S19 (RPS19), located at the head region of the 40S subunit. We suggest that this N-RPS19 interaction facilitates ribosome loading on capped mRNAs during N-mediated translation initiation.

scholarly journals Insulin is required for amino acid stimulation of dual pathways for translational control in skeletal muscle in the late-gestation ovine fetus

2009 ◽  
Vol 296 (1) ◽  
pp. E56-E63 ◽  
Author(s):  
Laura D. Brown ◽  
Paul J. Rozance ◽  
James S. Barry ◽  
Jacob E. Friedman ◽  
William W. Hay
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Amino Acid ◽  
Ribosomal Protein ◽  
Translation Initiation ◽  
Late Gestation ◽  
Acid Infusion ◽  
Amino Acid Infusion ◽  
Ribosomal Protein S6 ◽  
Ovine Fetus

During late gestation, amino acids and insulin promote skeletal muscle protein synthesis. However, the independent effects of amino acids and insulin on the regulation of mRNA translation initiation in the fetus are relatively unknown. The purpose of this study was to determine whether acute amino acid infusion in the late-gestation ovine fetus, with and without a simultaneous increase in fetal insulin concentration, activates translation initiation pathway(s) in skeletal muscle. Fetuses received saline (C), mixed amino acid infusion plus somatostatin infusion to suppress amino acid-stimulated fetal insulin secretion (AA+S), mixed amino acid infusion with concomitant physiological increase in fetal insulin (AA), or high-dose insulin infusion with euglycemia and euaminoacidemia (HI). After a 2-h infusion period, fetal skeletal muscle was harvested under in vivo steady-state conditions and frozen for quantification of proteins both upstream and downstream of mammalian target of rapamycin (mTOR). In the AA group, we found a threefold increase in ribosomal protein S6 kinase (p70S6k) and Erk1/2 phosphorylation; however, blocking the physiological rise in insulin with somatostatin in the AA+S group prevented this increase. In the HI group, Akt, Erk1/2, p70S6k, and ribosomal protein S6 were highly phosphorylated and 4E-binding protein 1 (4E-BP1) associated with eukaryotic initiation factor (eIF)4E decreased by 30%. These data show that insulin is a significant regulator of intermediates involved in translation initiation in ovine fetal skeletal muscle. Furthermore, the effect of amino acids is dependent on a concomitant increase in fetal insulin concentrations, because amino acid infusion upregulates p70S6k and Erk only when amino acid-stimulated increase in insulin occurs.

scholarly journals Noncanonical Translation Initiation Comes of Age

2017 ◽  
Vol 199 (14) ◽  
Author(s):  
Paul Babitzke ◽  
Michael O'Connor
Keyword(s):  
16S Rrna ◽  
Translation Initiation ◽  
Regulatory Mechanisms ◽  
Base Pairing ◽  
Initiation Mechanism ◽  
Link Type ◽  
Translation Initiation Mechanism

ABSTRACT The canonical translation initiation mechanism involves base pairing between the mRNA and 16S rRNA. However, a variety of identified mechanisms deviate from this conventional route. Beck and Janssen (J Bacteriol 199:e00091-17, 2017, https://doi.org/10.1128/JB.00091-17 ) have recently described another noncanonical mode of translation initiation. Here, we describe how this process differs from previously reported mechanisms, with the hope that it will foster increased awareness of the diversity of regulatory mechanisms that await discovery.

scholarly journals A Distinct Translation Initiation Mechanism Generates Cryptic Peptides for Immune Surveillance

PLoS ONE ◽  
2008 ◽  
Vol 3 (10) ◽  
pp. e3460 ◽  
Author(s):  
Shelley R. Starck ◽  
Yongkai Ow ◽  
Vivian Jiang ◽  
Maria Tokuyama ◽  
Mark Rivera ◽  
...  
Keyword(s):  
Translation Initiation ◽  
Immune Surveillance ◽  
Initiation Mechanism ◽  
Translation Initiation Mechanism
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