Designed Regular Tetragon-Shaped RNA–Protein Complexes with Ribosomal Protein L1 for Bionanotechnology and Synthetic Biology

ACS Nano ◽  
2015 ◽  
Vol 9 (5) ◽  
pp. 4950-4956 ◽  
Author(s):  
Hirohisa Ohno ◽  
Tan Inoue
Keyword(s):  
Synthetic Biology ◽  
Ribosomal Protein ◽  
Protein Complexes ◽  
Ribosomal Protein L1 ◽  
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.

scholarly journals Crystals of ribosomal protein L1 from a hyperthermophilic archaeon Methanococcus jannaschii

IUBMB Life ◽  
1998 ◽  
Vol 45 (2) ◽  
pp. 349-354
Author(s):  
Svetlana Tishchenko ◽  
Stanislav Nikonov ◽  
Maria Garber ◽  
Alex Kraft ◽  
Caroline Köhrer ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Methanococcus Jannaschii ◽  
Hyperthermophilic Archaeon ◽  
Ribosomal Protein L1

scholarly journals A mutant form of the ribosomal protein L1 reveals conformational flexibility

FEBS Letters ◽  
1997 ◽  
Vol 411 (1) ◽  
pp. 53-59 ◽  
Author(s):  
J Unge ◽  
S Al-Karadaghi ◽  
A Liljas ◽  
B.-H Jonsson ◽  
I Eliseikina ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Conformational Flexibility ◽  
Mutant Form ◽  
Ribosomal Protein L1

Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits

1993 ◽  
Vol 13 (5) ◽  
pp. 2835-2845
Author(s):  
M Deshmukh ◽  
Y F Tsay ◽  
A G Paulovich ◽  
J L Woolford
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Subunit ◽  
Single Copy ◽  
5S Rrna ◽  
Gene Encoding ◽  
Ribosomal Subunits ◽  
Ribosomal Protein L1 ◽  
The Stability ◽  
And Function

Ribosomal protein L1 from Saccharomyces cerevisiae binds 5S rRNA and can be released from intact 60S ribosomal subunits as an L1-5S ribonucleoprotein (RNP) particle. To understand the nature of the interaction between L1 and 5S rRNA and to assess the role of L1 in ribosome assembly and function, we cloned the RPL1 gene encoding L1. We have shown that RPL1 is an essential single-copy gene. A conditional null mutant in which the only copy of RPL1 is under control of the repressible GAL1 promoter was constructed. Depletion of L1 causes instability of newly synthesized 5S rRNA in vivo. Cells depleted of L1 no longer assemble 60S ribosomal subunits, indicating that L1 is required for assembly of stable 60S ribosomal subunits but not 40S ribosomal subunits. An L1-5S RNP particle not associated with ribosomal particles was detected by coimmunoprecipitation of L1 and 5S rRNA. This pool of L1-5S RNP remained stable even upon cessation of 60S ribosomal subunit assembly by depletion of another ribosomal protein, L16. Preliminary results suggest that transcription of RPL1 is not autogenously regulated by L1.

scholarly journals Isolation of Endogenously Assembled RNA-Protein Complexes Using Affinity Purification Based on Streptavidin Aptamer S1

2015 ◽  
Vol 16 (9) ◽  
pp. 22456-22472 ◽  
Author(s):  
Yangchao Dong ◽  
Jing Yang ◽  
Wei Ye ◽  
Yuan Wang ◽  
Chuantao Ye ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Affinity Purification ◽  
Streptavidin Aptamer ◽  
Rna Protein Complexes
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