Characterization of chemically induced mutations in the ad-1 locus of Schizosaccharomyces pombe

1973 ◽  
Vol 18 (1) ◽  
pp. 15-24 ◽  
Author(s):  
E. Segal ◽  
P. Munz ◽  
U. Leupold
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Induced Mutations ◽  
Chemically Induced

scholarly journals Construction and Characterization of Mutations within theKlebsiella mrkD1P Gene That Affect Binding to Collagen Type V

1999 ◽  
Vol 67 (4) ◽  
pp. 1672-1676 ◽  
Author(s):  
Tricia A. Sebghati ◽  
Steven Clegg
Keyword(s):  
Collagen Type ◽  
Gene Products ◽  
Induced Mutations ◽  
Binding Properties ◽  
Collagen Binding ◽  
Chemically Induced ◽  
Collagen Type V ◽  
Type V ◽  
Type 3

ABSTRACT The fimbria-associated MrkD1P protein mediates adherence of type 3 fimbriate strains of Klebsiella pneumoniae to collagen type V. Currently, three different MrkD adhesins have been described in Klebsiella species, and each possesses a distinctive binding pattern. Therefore, the binding abilities of mutants possessing defined mutations within themrkD 1P gene were examined in order to determine whether specific regions of the adhesin molecule were responsible for collagen binding. Both site-directed and chemically induced mutations were constructed within mrkD 1P, and the ability of the gene products to be incorporated into fimbrial appendages or bind to collagen was determined. Binding to type V collagen was not associated solely with one particular region of the MrkD1Pprotein, and two classes of nonadhesive mutants were isolated. In one class of mutants, the MrkD adhesin was not assembled into the fimbrial shaft, whereas in the second class of mutants, the adhesin was associated with fimbriae but did not bind to collagen. Both hemagglutinating and collagen-binding activities were associated with the MrkD1P molecule, since P pili and type 3 fimbriae carrying adhesive MrkD proteins exhibited identical binding properties.

Molecular characterization of radiation- and chemically induced mutations associated with neuromuscular tremors, runting, juvenile lethality, and sperm defects in jdf2 mice

1999 ◽  
Vol 10 (9) ◽  
pp. 870-878 ◽  
Author(s):  
Mitchell Walkowicz ◽  
Yonggang Ji ◽  
Xiaojia Ren ◽  
Bernhard Horsthemke ◽  
Liane B. Russell ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Induced Mutations ◽  
Chemically Induced

scholarly journals Direct Estimate of the Mutation Rate and the Distribution of Fitness Effects in the Yeast Saccharomyces cerevisiae

Genetics ◽  
2001 ◽  
Vol 159 (2) ◽  
pp. 441-452
Author(s):  
Dominika M Wloch ◽  
Krzysztof Szafraniec ◽  
Rhona H Borts ◽  
Ryszard Korona
Keyword(s):  
Spontaneous Mutation ◽  
Fruit Fly ◽  
Diploid Cell ◽  
Induced Mutations ◽  
Direct Estimate ◽  
Yeast Saccharomyces Cerevisiae ◽  
Related Trait ◽  
First Time ◽  
Defective Mismatch Repair

Abstract Estimates of the rate and frequency distribution of deleterious effects were obtained for the first time by direct scoring and characterization of individual mutations. This was achieved by applying tetrad analysis to a large number of yeast clones. The genomic rate of spontaneous mutation deleterious to a basic fitness-related trait, that of growth rate, was U = 1.1 × 10−3 per diploid cell division. Extrapolated to the fruit fly and humans, the per generation rate would be 0.074 and 0.92, respectively. This is likely to be an underestimate because single mutations with selection coefficients s < 0.01 could not be detected. The distribution of s ≥ 0.01 was studied both for spontaneous and induced mutations. The latter were induced by ethyl methanesulfonate (EMS) or resulted from defective mismatch repair. Lethal changes accounted for ~30–40% of the scored mutations. The mean s of nonlethal mutations was fairly high, but most frequently its value was between 0.01 and 0.05. Although the rate and distribution of very small effects could not be determined, the joint share of such mutations in decreasing average fitness was probably no larger than ~1%.

scholarly journals Characterization of Glycoside Hydrolase Family 5 Proteins in Schizosaccharomyces pombe

2010 ◽  
Vol 9 (11) ◽  
pp. 1650-1660 ◽  
Author(s):  
Encarnación Dueñas-Santero ◽  
Ana Belén Martín-Cuadrado ◽  
Thierry Fontaine ◽  
Jean-Paul Latgé ◽  
Francisco del Rey ◽  
...  
Keyword(s):  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Protein Characterization ◽  
Wall Material ◽  
Glycoside Hydrolase Family ◽  
Content Type ◽  
Hydrolysis Of ◽  
Controlled Hydrolysis ◽  
Hydrolase Family

ABSTRACT In yeast, enzymes with β-glucanase activity are thought to be necessary in morphogenetic events that require controlled hydrolysis of the cell wall. Comparison of the sequence of the Saccharomyces cerevisiae exo-β(1,3)-glucanase Exg1 with the Schizosaccharomyces pombe genome allowed the identification of three genes that were named exg1 + (locus SPBC1105.05), exg2 + (SPAC12B10.11), and exg3 + (SPBC2D10.05). The three proteins have different localizations: Exg1 is secreted to the periplasmic space, Exg2 is a membrane protein, and Exg3 is a cytoplasmic protein. Characterization of the biochemical activity of the proteins indicated that Exg1 and Exg3 are active only against β(1,6)-glucans while no activity was detected for Exg2. Interestingly, Exg1 cleaves the glucans with an endohydrolytic mode of action. exg1 + showed periodic expression during the cell cycle, with a maximum coinciding with the septation process, and its expression was dependent on the transcription factor Sep1. The Exg1 protein localizes to the septum region in a pattern that was different from that of the endo-β(1,3)-glucanase Eng1. Overexpression of Exg2 resulted in an increase in cell wall material at the poles and in the septum, but the putative catalytic activity of the protein was not required for this effect.

Identification and Characterization of the rhp23+ DNA Repair Gene in Schizosaccharomyces pombe

2000 ◽  
Vol 268 (1) ◽  
pp. 210-215 ◽  
Author(s):  
Marcel Lombaerts ◽  
Jerrelyne I. Goeloe ◽  
Hans den Dulk ◽  
Jourica A. Brandsma ◽  
Jaap Brouwer
Keyword(s):  
Dna Repair ◽  
Schizosaccharomyces Pombe ◽  
Repair Gene ◽  
Dna Repair Gene ◽  
Identification And Characterization

Partial characterization of an RNA component that copurifies with Saccharomyces cerevisiae RNase P

1989 ◽  
Vol 9 (6) ◽  
pp. 2536-2543
Author(s):  
J Y Lee ◽  
D R Engelke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Secondary Structure ◽  
Schizosaccharomyces Pombe ◽  
Rnase P ◽  
Partial Characterization ◽  
Rna Sequences ◽  
Extensive Sequence ◽  
Sequence Similarities

Saccharomyces cerevisiae cellular RNase P is composed of both protein and RNA components that are essential for activity. The isolated holoenzyme contains a highly structured RNA of 369 nucleotides that has extensive sequence similarities to the 286-nucleotide RNA associated with Schizosaccharomyces pombe RNase P but bears little resemblance to the analogous RNA sequences in procaryotes or S. cerevisiae mitochondria. Even so, the predicted secondary structure of S. cerevisiae RNA is strikingly similar to the bacterial phylogenetic consensus rather than to previously predicted structures of other eucaryotic RNase P RNAs.

Preparation and Characterization of γ-Fe2O3-ZnFe2O4 Composite Nanoparticles

2013 ◽  
Vol 873 ◽  
pp. 152-157
Author(s):  
Long Long Chen ◽  
Jun Ming Li ◽  
Xiao Min Gong ◽  
Jian Li
Keyword(s):  
Photoelectron Spectroscopy ◽  
Chemical Species ◽  
Composite Nanoparticles ◽  
X Ray Diffraction ◽  
Ferrite Core ◽  
Phase Synthesis ◽  
X Ray ◽  
Transmission Electron ◽  
Chemically Induced

Using a chemically induced transition in an FeCl2 solution, γ-Fe2O3 nanoparticles can be prepared from an amorphous precursor composed of FeOOH and Mg (OH)2. Surface modification by adding ZnCl2 during liquid-phase synthesis was attempted. The magnetization, morphology, crystal structure, and chemical species of as-prepared samples were characterized by vibrating sample magnetometer (VSM), transmission electron microscopy (TEM), X-ray diffraction (XRD), X-ray energy-dispersive spectroscopy (EDX), and X-ray photoelectron spectroscopy (XPS). The experimental results showed that the surface of the γ-Fe2O3 nanoparticles can be modified by adding ZnCl2 to form composite nanoparticles with a γ-Fe2O3/ZnFe2O4 ferrite core coated with Zn (OH)2 and absorbed FeCl36H2O; this modification can be enhanced by additional NaOH.

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