scholarly journals Co-expression of RNA–protein complexes in Escherichia coli and applications to RNA biology

2013 ◽  
Vol 41 (15) ◽  
pp. e150-e150 ◽  
Author(s):  
Luc Ponchon ◽  
Marjorie Catala ◽  
Bili Seijo ◽  
Marguerite El Khouri ◽  
Frédéric Dardel ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Complexes ◽  
Rna Biology ◽  
Rna Protein Complexes

Modeling the structure of the ribosome

1995 ◽  
Vol 73 (11-12) ◽  
pp. 751-756 ◽  
Author(s):  
Thomas R. Easterwood ◽  
Stephen C. Harvey
Keyword(s):  
Escherichia Coli ◽  
Protein Complexes ◽  
Small Subunit ◽  
Atomic Resolution ◽  
Molecular Models ◽  
Wide Range ◽  
30S Subunit ◽  
Resolution Model ◽  
Computer Based ◽  
Rna Protein Complexes

Considering the size and complexity of the ribosome and the growing body of data from a wide range of experiments on ribosomal structure, it is becoming increasingly important to develop tools that facilitate the development of reliable models for the ribosome. We use a combination of manual and computer-based approaches for building and refining models of the ribosome and other RNA–protein complexes. Our methods are aimed at determining the range of models compatible with the data, making quantitative statements about the positional uncertainties (resolution) of different regions, identifying conflicts in the data, establishing which regions of the ribosome need further experimental exploration, and, where possible, predicting the outcome of future experiments. Our previous low-resolution model for the small subunit of the Escherichia coli ribosome is briefly reviewed, along with progress on atomic resolution modeling of the mRNA–tRNA complex and its interaction with the decoding site of the 16S RNA.Key words: molecular models, 30S subunit, 16S decoding site, Escherichia coli, tRNA–mRNA complex.

Coexpression and Copurification of RNA–Protein Complexes in Escherichia coli

2021 ◽  
pp. 67-73
Author(s):  
Margot El Khouri ◽  
Marjorie Catala ◽  
Bili Seijo ◽  
Johana Chabal ◽  
Frédéric Dardel ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Complexes ◽  
Rna Protein Complexes

RNA and RNA–Protein Complex Crystallography and its Challenges

2014 ◽  
Vol 67 (12) ◽  
pp. 1741 ◽  
Author(s):  
Janine K. Flores ◽  
James L. Walshe ◽  
Sandro F. Ataide
Keyword(s):  
Protein Complex ◽  
Protein Complexes ◽  
Future Directions ◽  
Vast Number ◽  
X Ray Crystallography ◽  
Rna Biology ◽  
Non Coding Rnas ◽  
Rna Protein Complexes

RNA biology has changed completely in the past decade with the discovery of non-coding RNAs. Unfortunately, obtaining mechanistic information about these RNAs alone or in cellular complexes with proteins has been a major problem. X-ray crystallography of RNA and RNA–protein complexes has suffered from the major problems encountered in preparing and purifying them in large quantity. Here, we review the available techniques and methods in vitro and in vivo used to prepare and purify RNA and RNA–protein complex for crystallographic studies. We also discuss the future directions necessary to explore the vast number of RNA species waiting for their atomic-resolution structure to be determined.

Expression and Purification of RNA–Protein Complexes in Escherichia coli

2015 ◽  
pp. 25-31
Author(s):  
Margueritte El Khouri ◽  
Marjorie Catala ◽  
Bili Seijo ◽  
Johana Chabal ◽  
Carine Tisné ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Complexes ◽  
Expression And Purification ◽  
Rna Protein Complexes

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

scholarly journals Arabidopsis thaliana G3BP Ortholog Rescues Mammalian Stress Granule Phenotype across Kingdoms

2021 ◽  
Vol 22 (12) ◽  
pp. 6287
Author(s):  
Hendrik Reuper ◽  
Benjamin Götte ◽  
Lucy Williams ◽  
Timothy J. C. Tan ◽  
Gerald M. McInerney ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Fusion Proteins ◽  
Biological Function ◽  
Protein Complexes ◽  
Protein Family ◽  
Knock Out ◽  
Marker Proteins ◽  
Interaction Partners ◽  
Functional Analyses ◽  
Rna Protein Complexes

Stress granules (SGs) are dynamic RNA–protein complexes localized in the cytoplasm that rapidly form under stress conditions and disperse when normal conditions are restored. The formation of SGs depends on the Ras-GAP SH3 domain-binding protein (G3BP). Formations, interactions and functions of plant and human SGs are strikingly similar, suggesting a conserved mechanism. However, functional analyses of plant G3BPs are missing. Thus, members of the Arabidopsis thaliana G3BP (AtG3BP) protein family were investigated in a complementation assay in a human G3BP knock-out cell line. It was shown that two out of seven AtG3BPs were able to complement the function of their human homolog. GFP-AtG3BP fusion proteins co-localized with human SG marker proteins Caprin-1 and eIF4G1 and restored SG formation in G3BP double KO cells. Interaction between AtG3BP-1 and -7 and known human G3BP interaction partners such as Caprin-1 and USP10 was also demonstrated by co-immunoprecipitation. In addition, an RG/RGG domain exchange from Arabidopsis G3BP into the human G3BP background showed the ability for complementation. In summary, our results support a conserved mechanism of SG function over the kingdoms, which will help to further elucidate the biological function of the Arabidopsis G3BP protein family.

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