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.

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 Nucleotide sequence determination of guinea-pig casein B mRNA reveals homology with bovine and rat αs1 caseins and conservation of the non-coding regions of the mRNA.

1984 ◽  
Vol 222 (3) ◽  
pp. 561-570 ◽  
Author(s):  
L Hall ◽  
J E Laird ◽  
R K Craig
Keyword(s):  
Nucleotide Sequence ◽  
Guinea Pig ◽  
Nucleotide Sequence Analysis ◽  
Amino Acid Homology ◽  
Mrna Species ◽  
Cdna Sequences ◽  
Coding Regions ◽  
Casein Genes

Nucleotide sequence analysis of cloned guinea-pig casein B cDNA sequences has identified two casein B variants related to the bovine and rat alpha s1 caseins. Amino acid homology was largely confined to the known bovine or predicted rat phosphorylation sites and within the ‘signal’ precursor sequence. Comparison of the deduced nucleotide sequence of the guinea-pig and rat alpha s1 casein mRNA species showed greater sequence conservation in the non-coding than in the coding regions, suggesting a functional and possibly regulatory role for the non-coding regions of casein mRNA. The results provide insight into the evolution of the casein genes, and raise questions as to the role of conserved nucleotide sequences within the non-coding regions of mRNA species.

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.

THE ROLE OF ALKALINE PHOSPHATASE IN INTESTINAL ABSORPTION I. THE KINETICS OF PHOSPHATASE ACTION ON VARIOUS SUBSTRATES

1953 ◽  
Vol 31 (1) ◽  
pp. 1-7
Author(s):  
Neil B. Madsen ◽  
Jules Tuba
Keyword(s):  
Alkaline Phosphatase ◽  
Average Energy ◽  
Inorganic Phosphorus ◽  
Intestinal Alkaline Phosphatase ◽  
Egg Lecithin ◽  
Michaelis Constants ◽  
Inhibition Studies ◽  
Kinetics Of ◽  
Hydrolysis Of

The kinetics of intestinal alkaline phosphatase action on sodium β-glycerophosphate, glucose 6-phosphate, and egg lecithin have been studied and compared. The Michaelis constants indicate that the enzyme shows considerably less affinity for lecithin than for the other two substrates, and the approximate ratio of activity with lecithin, glucose 6-phosphate, and sodium β-glycerophosphate is 11 : 78.5 : 100. The energies of activation for the hydrolysis of the three substrates do not differ appreciably and the average energy of activation is 14,500 calories per gram-mole. The similarity of the energies of activation together with results from inhibition studies indicate that in all probability the same enzyme is responsible for the release of inorganic phosphorus from each of the three substrates.

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