Role of Ribosomal Protein L27 in Peptidyl Transfer†

Biochemistry ◽  
2008 ◽  
Vol 47 (17) ◽  
pp. 4898-4906 ◽  
Author(s):  
Stefan Trobro ◽  
Johan Åqvist
Keyword(s):  
Ribosomal Protein ◽  
Peptidyl Transfer

scholarly journals Role of the ribosomal protein L27 revealed by single-molecule FRET study

2012 ◽  
Vol 21 (11) ◽  
pp. 1696-1704 ◽  
Author(s):  
Yuhong Wang ◽  
Ming Xiao
Keyword(s):  
Ribosomal Protein ◽  
Single Molecule ◽  
Single Molecule Fret

scholarly journals Role of ribosomal protein mutations in tumor development (Review)

2016 ◽  
Vol 48 (4) ◽  
pp. 1313-1324 ◽  
Author(s):  
KAVEH M. GOUDARZI ◽  
MIKAEL S. LINDSTRÖM
Keyword(s):  
Ribosomal Protein ◽  
Tumor Development ◽  
Development Review ◽  
Protein Mutations

scholarly journals Ribosomal Protein L3 Mutants Alter Translational Fidelity and Promote Rapid Loss of the Yeast Killer Virus

1999 ◽  
Vol 19 (1) ◽  
pp. 384-391 ◽  
Author(s):  
Stuart W. Peltz ◽  
Amy B. Hammell ◽  
Ying Cui ◽  
Jason Yasenchak ◽  
Lara Puljanowski ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Missense Mutations ◽  
Ribosomal Frameshift ◽  
Virus Propagation ◽  
Particle Assembly ◽  
Ribosomal Frameshifting ◽  
Peptidyl Transfer ◽  
Yeast Killer ◽  
Peptidyltransferase Center ◽  
Killer Virus

ABSTRACT Programmed −1 ribosomal frameshifting is utilized by a number of RNA viruses as a means of ensuring the correct ratio of viral structural to enzymatic proteins available for viral particle assembly. Altering frameshifting efficiencies upsets this ratio, interfering with virus propagation. We have previously demonstrated that compounds that alter the kinetics of the peptidyl-transfer reaction affect programmed −1 ribosomal frameshift efficiencies and interfere with viral propagation in yeast. Here, the use of a genetic approach lends further support to the hypothesis that alterations affecting the ribosome’s peptidyltransferase activity lead to changes in frameshifting efficiency and virus loss. Mutations in theRPL3 gene, which encodes a ribosomal protein located at the peptidyltransferase center, promote approximately three- to fourfold increases in programmed −1 ribosomal frameshift efficiencies and loss of the M1 killer virus of yeast. Themak8-1 allele of RPL3 contains two adjacent missense mutations which are predicted to structurally alter the Mak8-1p. Furthermore, a second allele that encodes the N-terminal 100 amino acids of L3 (called L3Δ) exerts atrans-dominant effect on programmed −1 ribosomal frameshifting and killer virus maintenance. Taken together, these results support the hypothesis that alterations in the peptidyltransferase center affect programmed −1 ribosomal frameshifting.

Abstract 2864: Role of ribosomal protein, Rpl22 in regulation of acute lymphoblastic leukemia

2016 ◽  
Author(s):  
Nehal R. Solanki-Patel ◽  
Noa Greenberg ◽  
Shu Rao ◽  
Suraj Peri ◽  
Michael Slifker ◽  
...  
Keyword(s):  
Acute Lymphoblastic Leukemia ◽  
Ribosomal Protein ◽  
Lymphoblastic Leukemia

The functional role of the C-terminal tail of the human ribosomal protein uS19

2020 ◽  
Vol 1863 (3) ◽  
pp. 194490 ◽  
Author(s):  
Konstantin Bulygin ◽  
Alexey Malygin ◽  
Alexander Gopanenko ◽  
Dmitri Graifer ◽  
Galina Karpova
Keyword(s):  
Ribosomal Protein ◽  
Functional Role ◽  
Human Ribosomal Protein

scholarly journals Ubiquitin Extension Protein UEP1 Modulates Cell Death and Resistance to Various Pathogens in Tobacco

2019 ◽  
Vol 109 (7) ◽  
pp. 1257-1269
Author(s):  
You-Ping Xu ◽  
Yuan Zhao ◽  
Xiao-Yi Song ◽  
Yun-Feng Ye ◽  
Ren-Gang Wang ◽  
...  
Keyword(s):  
Cell Death ◽  
Disease Resistance ◽  
Ribosomal Protein ◽  
Mosaic Virus ◽  
Amine Oxidase ◽  
Active Species ◽  
26S Proteasome ◽  
Virus Induced Gene Silencing ◽  
Copper Amine Oxidase

Ubiquitin (Ub) extension proteins (UEPs) are fusion proteins of a Ub at the N terminus to a ribosomal protein. They are the main source of Ub and the only source of extension ribosomal protein. Although important roles of the Ub-26S proteasome system in various biological processes have been well established, direct evidence for the role of UEP genes in plant defense is rarely reported. In this study, we cloned a Ub-S27a-type UEP gene (NbUEP1) from Nicotiana benthamiana and demonstrated its function in cell death and disease resistance. Virus-induced gene silencing of NbUEP1 led to intensive cell death, culminating in whole-seedling withering. Transient RNA interference (RNAi) of NbUEP1 caused strong cell death in infiltrated areas, while stable NbUEP1-RNAi tobacco plants constitutively formed necrotic lesions in leaves. NbUEP1-RNAi plants exhibited increased resistance to the oomycete Pythium aphanidermatum and viruses Tobacco mosaic virus and Cucumber mosaic virus while displaying decreased resistance to the nematode Meloidogyne incognita compared with non-RNAi control plants. Transcription profiling analysis indicated that jasmonate and ethylene pathways, lipid metabolism, copper amine oxidase-mediated active species generation, glycine-rich proteins, vacuolar processing enzyme- and RD21-mediated cell death and defense regulation, and autophagy might be associated with NbUEP1-mediated cell death and resistance. Our results provided evidence for the important roles of plant UEPs in modulating plant cell death and disease resistance.

scholarly journals Mutations in Ribosomal Protein L16 Conferring Reduced Susceptibility to Evernimicin (SCH27899): Implications for Mechanism of Action

2000 ◽  
Vol 44 (3) ◽  
pp. 732-738 ◽  
Author(s):  
Peter V. Adrian ◽  
Wenjun Zhao ◽  
Todd A. Black ◽  
Karen J. Shaw ◽  
Roberta S. Hare ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Linear Response ◽  
Rapid Decrease ◽  
Nucleotide Sequence Analysis ◽  
Secondary Effects ◽  
Direct Transformation ◽  
Susceptible Isolate ◽  
Inhibitor Of Protein Synthesis ◽  
Inhibition Studies

ABSTRACT A clinical isolate of Streptococcus pneumoniae (SP#5) that showed decreased susceptibility to evernimicin (MIC, 1.5 μg/ml) was investigated. A 4,255-bp EcoRI fragment cloned from SP#5 was identified by its ability to transform evernimicin-susceptibleS. pneumoniae R6 (MIC, 0.03 μg/ml) such that the evernimicin MIC was 1.5 μg/ml. Nucleotide sequence analysis of this fragment revealed that it contained portions of the S10-spc ribosomal protein operons. The nucleotide sequences of resistant and susceptible isolates were compared, and a point mutation (thymine to guanine) that causes an Ile52-Ser substitution in ribosomal protein L16 was identified. The role of this mutation in decreasing susceptibility to evernimicin was confirmed by direct transformation of the altered L16 gene. The presence of the L16 mutation in the resistant strain suggests that evernimicin is an inhibitor of protein synthesis. This was confirmed by inhibition studies using radiolabeled substrates, which showed that the addition of evernimicin at sub-MIC levels resulted in a rapid decrease in the incorporation of radiolabeled isoleucine in a susceptible isolate (SP#3) but was much less effective against SP#5. The incorporation of isoleucine showed a linear response to the dose level of evernimicin. The incorporation of other classes of labeled substrates was unaffected or much delayed, indicating that these were secondary effects.

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