Structure and role of 5S RNA-protein complexes in protein biosynthesis

1981 ◽  
Vol 6 ◽  
pp. 137-139 ◽  
Author(s):  
R.A. Garrett ◽  
S. Douthwaite ◽  
H.F. Noller
Keyword(s):  
Protein Complexes ◽  
Protein Biosynthesis ◽  
5S Rna ◽  
Rna Protein Complexes

The 5S RNA – protein complex from yeast: a model for the evolution and structure of the eukaryotic ribosome

1982 ◽  
Vol 60 (4) ◽  
pp. 490-496 ◽  
Author(s):  
Ross N. Nazar ◽  
Makoto Yaguchi ◽  
Gordon E. Willick
Keyword(s):  
Binding Site ◽  
Protein Complex ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Protein Complexes ◽  
Basic Structure ◽  
5S Rna ◽  
Chemical Studies ◽  
Physical And Chemical ◽  
Rna Protein Complexes

The ribosomal 5S RNA – protein complex appears to be an excellent model for studies on the evolution and structure of ribosomes. In eukaryotes this complex is composed of two components, the 5S rRNA and a single ribosomal protein which in yeast has a molecular weight of about 38 000. The primary protein-binding site is located in the 3′-end region of the 5S RNA together with a small portion of the 5′ end. The primary RNA-binding site appears to be situated in the C-terminal end of the protein (YL3 in yeast) but the binding specificity requires other structural elements in the N-terminal half of the molecule. When compared with prokaryotic 5S RNA – protein complexes, various physical and chemical studies suggest that the basic structure and interactions have been conserved in the course of evolution, but that the single larger eukaryotic 5S RNA binding protein has evolved through a fusion of genes for the multiple 5S RNA binding proteins in prokaryotes.

scholarly journals Granule regulation by phase separation during Drosophila oogenesis

2020 ◽  
Vol 4 (3) ◽  
pp. 355-364
Author(s):  
M. Sankaranarayanan ◽  
Timothy T. Weil
Keyword(s):  
Phase Separation ◽  
Translational Control ◽  
Protein Complexes ◽  
Physiological Role ◽  
Drosophila Oogenesis ◽  
And Function ◽  
Rna Protein Complexes ◽  
Liquid Liquid Phase Separation

Drosophila eggs are highly polarised cells that use RNA–protein complexes to regulate storage and translational control of maternal RNAs. Ribonucleoprotein granules are a class of biological condensates that form predominantly by intracellular phase separation. Despite extensive in vitro studies testing the physical principles regulating condensates, how phase separation translates to biological function remains largely unanswered. In this perspective, we discuss granules in Drosophila oogenesis as a model system for investigating the physiological role of phase separation. We review key maternal granules and their properties while highlighting ribonucleoprotein phase separation behaviours observed during development. Finally, we discuss how concepts and models from liquid–liquid phase separation could be used to test mechanisms underlying granule assembly, regulation and function in Drosophila oogenesis.

scholarly journals Base-intercalated and base-wedged stacking elements in 3D-structure of RNA and RNA–protein complexes

2020 ◽  
Vol 48 (15) ◽  
pp. 8675-8685
Author(s):  
Eugene Baulin ◽  
Valeriy Metelev ◽  
Alexey Bogdanov
Keyword(s):  
Tertiary Structure ◽  
Protein Complexes ◽  
3D Structure ◽  
Data Bank ◽  
Rna Structures ◽  
Tertiary Structures ◽  
Long Range Interactions ◽  
Heterocyclic Bases ◽  
Rna Protein Complexes

Abstract Along with nucleobase pairing, base-base stacking interactions are one of the two main types of strong non-covalent interactions that define the unique secondary and tertiary structure of RNA. In this paper we studied two subfamilies of nucleobase-inserted stacking structures: (i) with any base intercalated between neighboring nucleotide residues (base-intercalated element, BIE, i + 1); (ii) with any base wedged into a hydrophobic cavity formed by heterocyclic bases of two nucleotides which are one nucleotide apart in sequence (base-wedged element, BWE, i + 2). We have exploited the growing database of natively folded RNA structures in Protein Data Bank to analyze the distribution and structural role of these motifs in RNA. We found that these structural elements initially found in yeast tRNAPhe are quite widespread among the tertiary structures of various RNAs. These motifs perform diverse roles in RNA 3D structure formation and its maintenance. They contribute to the folding of RNA bulges and loops and participate in long-range interactions of single-stranded stretches within RNA macromolecules. Furthermore, both base-intercalated and base-wedged motifs participate directly or indirectly in the formation of RNA functional centers, which interact with various ligands, antibiotics and proteins.

scholarly journals Fructose modulates GLUT5 mRNA stability in differentiated Caco-2 cells: role of cAMP-signalling pathway and PABP (polyadenylated-binding protein)-interacting protein (Paip) 2

2003 ◽  
Vol 375 (1) ◽  
pp. 167-174 ◽  
Author(s):  
Florence GOUYON ◽  
Cercina ONESTO ◽  
Veronique DALET ◽  
Gilles PAGES ◽  
Armelle LETURQUE ◽  
...  
Keyword(s):  
Mrna Stability ◽  
Protein Complexes ◽  
Binding Protein ◽  
Interacting Protein ◽  
Camp Signalling ◽  
Camp Pathway ◽  
Post Transcriptional Regulation ◽  
Rna Protein Complexes ◽  
Camp Levels

In intestinal cells, levels of the fructose transporter GLUT5 are increased by glucose and to a greater extent by fructose. We investigated the mechanism by which fructose increases GLUT5 expression. In Caco-2 cells, fructose and glucose increased activity of the −2500/+41 GLUT5 promoter to the same extent. cAMP also activated the GLUT5 promoter. However, if a protein kinase A inhibitor was used to block cAMP signalling, extensive GLUT5 mRNA degradation was observed, with no change in basal transcription levels demonstrating the involvement of cAMP in GLUT5 mRNA stability. Indeed, the half-life of GLUT5 mRNA was correlated (R2=0.9913) with cellular cAMP levels. Fructose increased cAMP concentration more than glucose, accounting for the stronger effect of fructose when compared with that of glucose on GLUT5 production. We identified several complexes between GLUT5 3′-UTR RNA (where UTR stands for untranslated region) and cytosolic proteins that might participate in mRNA processing. Strong binding of a 140 kDa complex I was observed in sugar-deprived cells, with levels of binding lower in the presence of fructose and glucose by factors of 12 and 6 respectively. This may account for differences in the effects of fructose and glucose. In contrast, the amounts of two complexes of 96 and 48 kDa increased equally after stimulation with either glucose or fructose. Finally, PABP (polyadenylated-binding protein)-interacting protein 2, a destabilizing partner of PABP, was identified as a component of GLUT5 3′-UTR RNA–protein complexes. We conclude that the post-transcriptional regulation of GLUT5 by fructose involves increases in mRNA stability mediated by the cAMP pathway and Paip2 (PABP-interacting protein 2) binding.

The emerging role of MS in structure elucidation of protein–nucleic acid complexes

2008 ◽  
Vol 36 (4) ◽  
pp. 723-731 ◽  
Author(s):  
Yuliya Gordiyenko ◽  
Carol V. Robinson
Keyword(s):  
Nucleic Acid ◽  
High Resolution ◽  
Structural Biology ◽  
Structure Elucidation ◽  
Protein Complexes ◽  
Subunit Interactions ◽  
Protein Nucleic Acid ◽  
Architectural Organization ◽  
Rna Protein Complexes

Developments in MS enable us to apply this technique to non-covalent complexes, defining their stoichiometry, subunit interactions and architectural organization. We illustrate the application of this non-covalent MS approach to uncovering the overall topological arrangements of subunits and interactions within RNA–protein complexes studied in our laboratory over the last 5 years. These studies exemplify the emerging role and potential of MS as a complementary structural biology methodology and demonstrate its unique niche in investigations of dynamic or heterogeneous protein–nucleic acid complexes, which are not accessible to classical high-resolution structural biology techniques.

scholarly journals Alu RNA-protein complexes formed in vitro react with a novel lupus autoantibody.

1985 ◽  
Vol 260 (21) ◽  
pp. 11781-11786
Author(s):  
R Kole ◽  
L D Fresco ◽  
J D Keene ◽  
P L Cohen ◽  
R A Eisenberg ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Alu Rna ◽  
Rna Protein Complexes
Sign in / Sign up

Export Citation Format

Share Document