Crystal Structure of Ribosomal Protein L30e from the Extreme ThermophileThermococcus celer:  Thermal Stability and RNA Binding†,‡

Biochemistry ◽  
2003 ◽  
Vol 42 (10) ◽  
pp. 2857-2865 ◽  
Author(s):  
Yu Wai Chen ◽  
Mark Bycroft ◽  
Kam-Bo Wong
Keyword(s):  
Crystal Structure ◽  
Thermal Stability ◽  
Ribosomal Protein ◽  
Rna Binding

scholarly journals Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein.

1994 ◽  
Vol 13 (1) ◽  
pp. 205-212 ◽  
Author(s):  
D.W. Hoffman ◽  
C. Davies ◽  
S.E. Gerchman ◽  
J.H. Kycia ◽  
S.J. Porter ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ribosomal Protein ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Ribosomal Protein L9

scholarly journals The Contribution of Ribosomal Protein S1 to the Structure and Function of Qβ Replicase

Acta Naturae ◽  
2017 ◽  
Vol 9 (4) ◽  
pp. 26-30
Author(s):  
Z. Sh. Kutlubaeva ◽  
Е. V. Chetverina ◽  
A. B. Chetverin
Keyword(s):  
Crystal Structure ◽  
Ribosomal Protein ◽  
Rna Binding ◽  
Structure And Function ◽  
Ribosomal Protein S1 ◽  
Bacterial Ribosome ◽  
New Findings ◽  
Replicase Complex ◽  
And Function ◽  
Fixed Structure

The high resolution crystal structure of bacterial ribosome was determined more than 10 years ago; however, it contains no information on the structure of the largest ribosomal protein, S1. This unusual protein comprises six flexibly linked domains; therefore, it lacks a fixed structure and this prevents the formation of crystals. Besides being a component of the ribosome, protein S1 also serves as one of the four subunits of Q replicase, the RNA-directed RNA polymerase of bacteriophage Q. In each case, the role of this RNA-binding protein has been thought to consist in holding the template close to the active site of the enzyme. In recent years, a breakthrough was made in studies of protein S1 within Q replicase. This includes the discovery of its paradoxical ability to displace RNA from the replicase complex and determining the crystal structure of its fragment capable of performing this function. The new findings call for a re-examination of the contribution of protein S1 to the structure and function of the ribosome.

scholarly journals Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus.

1996 ◽  
Vol 15 (6) ◽  
pp. 1350-1359 ◽  
Author(s):  
S. Nikonov ◽  
N. Nevskaya ◽  
I. Eliseikina ◽  
N. Fomenkova ◽  
A. Nikulin ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ribosomal Protein ◽  
Rna Binding ◽  
Thermus Thermophilus ◽  
Ribosomal Protein L1

Crystal structure of ribosomal protein S8 from Thermus thermophilus reveals a high degree of structural conservation of a specific RNA binding site 1 1Edited by K. Nagai

1998 ◽  
Vol 279 (1) ◽  
pp. 233-244 ◽  
Author(s):  
Natalia Nevskaya ◽  
Svetlana Tishchenko ◽  
Alexei Nikulin ◽  
Salam Al-Karadaghi ◽  
Anders Liljas ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ribosomal Protein ◽  
Binding Site ◽  
Rna Binding ◽  
Thermus Thermophilus ◽  
Structural Conservation ◽  
High Degree

scholarly journals Requirement for C-terminal Extension to the RNA Binding Domain for Efficient RNA Binding by Ribosomal Protein L2

2002 ◽  
Vol 66 (3) ◽  
pp. 682-684 ◽  
Author(s):  
Takeshi HAYASHI ◽  
Maino TAHARA ◽  
Kenta IWASAKI ◽  
Yoshiaki KOUZUMA ◽  
Makoto KIMURA
Keyword(s):  
Ribosomal Protein ◽  
Rna Binding ◽  
Binding Domain ◽  
Ribosomal Protein L2 ◽  
Rna Binding Domain

scholarly journals Experimental Selection of Paromomycin Resistance in Leishmania donovani Amastigotes Induces Variable Genomic Polymorphisms

2021 ◽  
Vol 9 (8) ◽  
pp. 1546
Author(s):  
Sarah Hendrickx ◽  
João Luís Reis-Cunha ◽  
Sarah Forrester ◽  
Daniel C. Jeffares ◽  
Guy Caljon
Keyword(s):  
Ribosomal Protein ◽  
Protein Tyrosine Phosphatase ◽  
Copy Number ◽  
Leishmania Donovani ◽  
Rna Binding ◽  
Tyrosine Phosphatase ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Gene Copy ◽  
Protein Tyrosine

The relatively high post-treatment relapse rates of paromomycin (PMM) in visceral leishmaniasis treatment and the swift emergence of experimental drug resistance challenge its broad application and urge for rational use and monitoring of resistance. However, no causal molecular mechanisms to Leishmania PMM resistance have been identified so far. To gain insights into potential resistance mechanisms, twelve experimentally selected Leishmania donovani clonal lines and the non-cloned preselection population, with variable degrees of PMM resistance, were subjected to whole genome sequencing. To identify genomic variations potentially associated with resistance, SNPs, Indels, chromosomal somy and gene copy number variations were compared between the different parasite lines. A total of 11 short nucleotide variations and the copy number alterations in 39 genes were correlated to PMM resistance. Some of the identified genes are involved in transcription, translation and protein turn-over (transcription elongation factor-like protein, RNA-binding protein, ribosomal protein L1a, 60S ribosomal protein L6, eukaryotic translation initiation factor 4E-1, proteasome regulatory non-ATP-ase subunit 3), virulence (major surface protease gp63, protein-tyrosine phosphatase 1-like protein), mitochondrial function (ADP/ATP mitochondrial carrier-like protein), signaling (phosphatidylinositol 3-related kinase, protein kinase putative and protein-tyrosine phosphatase 1-like protein) and vesicular trafficking (ras-related protein RAB1). These results indicate that, in Leishmania, the aminoglycoside PMM affects protein translational processes and underlines the complex and probably multifactorial origin of resistance.

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