Cross-Linkage by “Intact” Bizelesin and Bisalkylation by the “Separated Halves” of the Bizelesin Dimer:  Contrasting Drug Manipulation of DNA Conformation (5‘-TAATTA-3‘) Directs Alkylation toward Different Adenine Targets

1996 ◽  
Vol 118 (23) ◽  
pp. 5383-5395 ◽  
Author(s):  
Frederick C. Seaman ◽  
Jianxiong Chu ◽  
Laurence Hurley
Author(s):  
Masaatsu Koike ◽  
Koichi Nakashima ◽  
Kyoko Iida

Penicillin exerts the activity to inhibit the peptide cross linkage between each polysaccharide backbone at the final stage of wall-peptidoglycan biosynthesis of bacteria. Morphologically, alterations of the septal wall and mesosome in gram-positive bacteria, which were occurred in early time after treatment with penicillin, have been observed. In this experiment, these alterations were cytochemically investigated by means of silver-methenamine staining after periodate oxidation, which is applied for detection of localization of wall mucopolysaccharide.Staphylococcus aureus strain 209P treated with 100 u/ml of penicillin G was divided into two aliquotes. One was fixed by Kellenberger-Ryter's OSO4 fixative at 30, 60 and 120 min after addition of the antibiotic, dehydrated through alcohol series, and embedded in Epon 812 (Specimen A). The other was fixed by 21 glutaraldehyde, dehydrated through glycolmethacrylate series and embedded in glycolmethacrylate mixture, according to Bernhard's method (Specimen B).


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Ruifang Guan ◽  
Tengfei Lian ◽  
Bing-Rui Zhou ◽  
Emily He ◽  
Carl Wu ◽  
...  

AbstractAccurate chromosome segregation relies on the specific centromeric nucleosome–kinetochore interface. In budding yeast, the centromere CBF3 complex guides the deposition of CENP-A, an H3 variant, to form the centromeric nucleosome in a DNA sequence-dependent manner. Here, we determine the structures of the centromeric nucleosome containing the native CEN3 DNA and the CBF3core bound to the canonical nucleosome containing an engineered CEN3 DNA. The centromeric nucleosome core structure contains 115 base pair DNA including a CCG motif. The CBF3core specifically recognizes the nucleosomal CCG motif through the Gal4 domain while allosterically altering the DNA conformation. Cryo-EM, modeling, and mutational studies reveal that the CBF3core forms dynamic interactions with core histones H2B and CENP-A in the CEN3 nucleosome. Our results provide insights into the structure of the budding yeast centromeric nucleosome and the mechanism of its assembly, which have implications for analogous processes of human centromeric nucleosome formation.


1987 ◽  
Vol 42 (11-12) ◽  
pp. 1165-1170 ◽  
Author(s):  
Uwe J. Jürgens ◽  
Baldur Rieth ◽  
Jürgen Weckesser ◽  
Crawford S. Dow ◽  
Wilfried A. König

The rigid layer and peptidoglycan fractions from two strains (ATCC 17100 and Rm 5) of the budding phototrophic Rhodomicrobium vannielii were isolated. Rigid layers of both strains contain protein in addition to peptidoglycan. They were free of polysaccharides and fatty acids. The respective peptidoglycan fractions contain glucosamine, muramic acid, ʟ-and ᴅ-alanine, ᴅ-glutamic and meso-diaminopimelic acid in approximately equimolar ratios except for a signifi­ cant lower relative ᴅ-alanine content. Analysis of partial acid hydrolysates revealed A 1 γ-type structure of Rhodomicrobium vannielii peptidoglycan (shown with strain ATCC 17100). An about 10-30% lack of N-acetylation of glucosamine was indicated. The degree of cross-linkage was found to be about 60% . No differences in peptidoglycan composition and degree of cross-linkage were found between swarmer-and chain-cells as examined with strain Rm 5.


2021 ◽  
Vol 11 (13) ◽  
pp. 5895
Author(s):  
Kristina Serec ◽  
Sanja Dolanski Babić

The double-stranded B-form and A-form have long been considered the two most important native forms of DNA, each with its own distinct biological roles and hence the focus of many areas of study, from cellular functions to cancer diagnostics and drug treatment. Due to the heterogeneity and sensitivity of the secondary structure of DNA, there is a need for tools capable of a rapid and reliable quantification of DNA conformation in diverse environments. In this work, the second paper in the series that addresses conformational transitions in DNA thin films utilizing FTIR spectroscopy, we exploit popular chemometric methods: the principal component analysis (PCA), support vector machine (SVM) learning algorithm, and principal component regression (PCR), in order to quantify and categorize DNA conformation in thin films of different hydrated states. By complementing FTIR technique with multivariate statistical methods, we demonstrate the ability of our sample preparation and automated spectral analysis protocol to rapidly and efficiently determine conformation in DNA thin films based on the vibrational signatures in the 1800–935 cm−1 range. Furthermore, we assess the impact of small hydration-related changes in FTIR spectra on automated DNA conformation detection and how to avoid discrepancies by careful sampling.


1977 ◽  
Vol 131 ◽  
pp. 91-97 ◽  
Author(s):  
Anna Goździcka-Józefiak ◽  
Jacek Augustyniak
Keyword(s):  

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