scholarly journals Novel nucleotide mutation leading to a recurrent amino acid alteration inSH3BP2in a patient with cherubism

2013 ◽  
Vol 53 (4) ◽  
pp. 166-169 ◽  
Author(s):  
Noriko Sangu ◽  
Tsuyoshi Shimosato ◽  
Hirosato Inoda ◽  
Shino Shimada ◽  
Keiko Shimojima ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nucleotide Mutation ◽  
Acid Alteration ◽  
Amino Acid Alteration

scholarly journals A Single Amino Acid Alteration in PGR5 Confers Resistance to Antimycin A in Cyclic Electron Transport around PSI

2013 ◽  
Vol 54 (9) ◽  
pp. 1525-1534 ◽  
Author(s):  
Kazuhiko Sugimoto ◽  
Yuki Okegawa ◽  
Akihiko Tohri ◽  
Terri A. Long ◽  
Sarah F. Covert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Electron Transport ◽  
Single Amino Acid ◽  
Antimycin A ◽  
Cyclic Electron Transport ◽  
Acid Alteration ◽  
Amino Acid Alteration

scholarly journals Target of rapamycin signalling mediates the lifespan-extending effects of dietary restriction by essential amino acid alteration

Aging ◽  
2014 ◽  
Vol 6 (5) ◽  
pp. 390-398 ◽  
Author(s):  
Sahar Emran ◽  
Mingyao Yang ◽  
Xiaoli He ◽  
Jelle Zandveld ◽  
Matthew D. W. Piper
Keyword(s):  
Amino Acid ◽  
Dietary Restriction ◽  
Essential Amino Acid ◽  
Target Of Rapamycin ◽  
Acid Alteration ◽  
Amino Acid Alteration

Highlights Plasma and Muscle Free Amino Acid Alteration in Uremic Children

1981 ◽  
pp. 267-268
Author(s):  
Michel Broyer ◽  
G. Jean ◽  
C. Kleinknecht ◽  
A. M. Dartois ◽  
F. Gros
Keyword(s):  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino ◽  
Acid Alteration ◽  
Amino Acid Alteration

Acquisition of Certain Streptomycin-Resistant (str) Mutations Enhances Antibiotic Production in Bacteria

1998 ◽  
Vol 42 (8) ◽  
pp. 2041-2047 ◽  
Author(s):  
Yoshiko Hosoya ◽  
Susumu Okamoto ◽  
Hideyuki Muramatsu ◽  
Kozo Ochi
Keyword(s):  
Amino Acid ◽  
Antibiotic Production ◽  
Gene Replacement ◽  
Rational Approach ◽  
Increase In Productivity ◽  
Adverse Environmental Conditions ◽  
Ribosomal Protein S12 ◽  
Acid Alteration ◽  
Type Strains ◽  
Amino Acid Alteration

ABSTRACT Physiological differentiation (including antibiotic production) in microorganisms usually starts when cells encounter adverse environmental conditions and is frequently accompanied by an increase in the accumulation of intracellular ppGpp. We have found that the acquisition of certain streptomycin-resistant (str) mutations enables cells to overproduce antibiotics, demonstrating an increase in productivity 5- to 50-fold greater than that of wild-type strains. The frequency of such antibiotic-overproducing strains among the str mutants was shown to range from 3 to 46%, as examined with several strains of the genera Streptomyces,Bacillus, and Pseudomonas. Analysis of str mutants from Bacillus subtilisMarburg 168 revealed that a point mutation occurred within therpsL gene, which encodes the ribosomal protein S12, changing Lys-56 (corresponding to Lys-43 in Escherichia coli) to Asn, Arg, Thr, or Gln. Antibiotic productivity increased in a hierarchical manner depending upon which amino acid residue replaced Lys at this position. The strA1 mutation, a genetic marker frequently used for mapping, had no effect on antibiotic productivity even though it was found to result in an amino acid alteration of Lys-56 to Ile. Gene replacement experiments with thestr alleles demonstrated unambiguously that thestr mutation is responsible for the antibiotic overproductivity observed. These results offer a rational approach for improving the production of antibiotic (secondary metabolism) from microorganisms.

scholarly journals Ribosomal Mutations Conferring Resistance to Macrolides in Streptococcus pneumoniae Clinical Strains Isolated in Germany

2003 ◽  
Vol 47 (7) ◽  
pp. 2319-2322 ◽  
Author(s):  
Ralf René Reinert ◽  
Angela Wild ◽  
Peter Appelbaum ◽  
Rudolf Lütticken ◽  
Murat Yücel Cil ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Amino Acid ◽  
Ribosomal Protein ◽  
Macrolide Resistance ◽  
23S Rrna ◽  
Resistance Phenotype ◽  
Clinical Strains ◽  
Acid Alteration ◽  
Amino Acid Alteration

ABSTRACT Among a collection of 4,281 pneumococcal isolates, 7 strains isolated in Germany had an unusual macrolide resistance phenotype. The isolates were found to have multiple mutations in the 23S rRNA and alterations in the L4 ribosomal protein. One strain had an amino acid alteration in the L22 ribosomal protein.

scholarly journals A Single Amino Acid Alteration in the Human Parainfluenza Virus Type 3 Hemagglutinin-Neuraminidase Glycoprotein Confers Resistance to the Inhibitory Effects of Zanamivir on Receptor Binding and Neuraminidase Activity

2001 ◽  
Vol 75 (14) ◽  
pp. 6310-6320 ◽  
Author(s):  
Matthew T. Murrell ◽  
Matteo Porotto ◽  
Olga Greengard ◽  
Natalia Poltoratskaia ◽  
Anne Moscona
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Virus Type ◽  
Parainfluenza Virus ◽  
Single Amino Acid ◽  
Plaque Morphology ◽  
Human Parainfluenza Virus ◽  
Type 3 ◽  
Acid Alteration ◽  
Amino Acid Alteration

ABSTRACT Entry and fusion of human parainfluenza virus type 3 (HPF3) requires interaction of the viral hemagglutinin-neuraminidase (HN) glycoprotein with its sialic acid receptor. 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid (4-GU-DANA; zanamivir), a sialic acid transition-state analog designed to fit the influenza virus neuraminidase catalytic site, possesses antiviral activity at nanomolar concentrations in vitro. We have shown previously that 4-GU-DANA also inhibits both HN-mediated binding of HPF3 to host cell receptors and HN's neuraminidase activity. In the present study, a 4-GU-DANA-resistant HPF3 virus variant (ZM1) was generated by serial passage in the presence of 4-GU-DANA. ZM1 exhibited a markedly fusogenic plaque morphology and harbored two HN gene mutations resulting in two amino acid alterations, T193I and I567V. Another HPF3 variant studied in parallel, C-0, shared an alteration at T193 and exhibited similar plaque morphology but was not resistant to 4-GU-DANA. Neuraminidase assays revealed a 15-fold reduction in 4-GU-DANA sensitivity for ZM1 relative to the wild type (WT) and C-0. The ability of ZM1 to bind sialic acid receptors was inhibited 10-fold less than for both WT and C-0 in the presence of 1 mM 4-GU-DANA. ZM1 also retained infectivity at 15-fold-higher concentrations of 4-GU-DANA than WT and C-0. A single amino acid alteration at HN residue 567 confers these 4-GU-DANA-resistant properties. An understanding of ZM1 and other escape variants provides insight into the effects of this small molecule on HN function as well as the role of the HN glycoprotein in HPF3 pathogenesis.

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