Exhaustive EcoRI digests of circular dimer mitochondrial DNA (mtDNA) from mouse cell lines LD and LDTK- yield two major fragments whose average lengths are slightly smaller than the corresponding fragments of circular monomer mtDNA from mouse LA9 and LMTK- cells. A third fragment approximately 400 nucleotide pairs in length is frequently produced in less than molar yield. Exhaustive EcoRI digests of circular dimer mtDNA from human acute myelogenous leukemic leucocytes yield three major fragments. The presence of mtDNA resistant to cleavage as well as fragments of intermediate sizes indicatesmicroheterogeneity in the genomic positions of EcoRI recognition sequences in both mouse and human circular dimer mtDNA. Analysis of the distribution averages of circular contour lengths indicates microheterogeneity in the sizes of mouse LD and human mtDNAs. The denatured-renatured EcoRI fragments frequently contain a small loop(s) of single-strand DNA as would occur for deletion(s) or addition(s) of single-strand DNA as would occur for deletion(s) or addition(s) of nucleotide sequences in some of the circular dimer molecules.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC343758PMC
http://dx.doi.org/10.1093/nar/4.5.1315DOI Listing

Publication Analysis

Top Keywords

circular dimer
20
dimer mitochondrial
8
mitochondrial dna
8
exhaustive ecori
8
ecori digests
8
digests circular
8
mtdna mouse
8
major fragments
8
dimer mtdna
8
mouse human
8

Similar Publications

Monoclonal antibodies recognizing nonprotein antigens remain largely underrepresented in our understanding of the molecular repertoire of innate and adaptive immunity. One such antibody is Mannitou, a murine IgM that recognizes paucimannosidic glycans. In this work, we report the production and purification of the recombinant antigen-binding fragment (Fab) of Mannitou IgM (Mannitou Fab) and employ a combination of biochemical and biophysical approaches to obtain its initial structural characterization.

View Article and Find Full Text PDF

SARS-CoV-2 continues to mutate, leading to breakthrough infections. The development of new vaccine strategies to combat various strains is crucial. Protein cyclization can enhance thermal stability and may improve immunogenicity.

View Article and Find Full Text PDF

We report the synthesis and characterization of two chiral binuclear iridium(III) complexes ( and ) prepared from enantiopure building blocks [μ-Cl(Δ-Ir(C^N))] and [μ-Cl(Λ-Ir(C^N))]. These building blocks have been obtained by chiral preparative high-performance liquid chromatography of the neutral iridium(III) complex (piv = 2,2,6,6-tetramethylheptane-3,5-dionate) followed by selective degradation of the ancillary ligand. For comparison purposes, we also synthesized a monomer () and a dimer (, mixture).

View Article and Find Full Text PDF

Plasmon chirality has garnered significant interest in sensing application due to its strong electromagnetic field localization and highly tunable optical properties. Understanding the effects of mode coupling in chiral structures on chiral optical activity is particularly important for advancing this field. In this work, we numerically investigate the circular dichroism (CD) of elliptical nanodisk dimers arranged in an up-and-down configuration with a specific rotation angle.

View Article and Find Full Text PDF

Assembly landscape of the complete B-repeat superdomain from Staphylococcus epidermidis strain 1457.

Biophys J

December 2024

Division of Immunobiology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, USA; Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, USA; Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH, USA. Electronic address:

The accumulation-associated protein (Aap) is the primary determinant of Staphylococcus epidermidis device-related infections. The B-repeat superdomain is responsible for intercellular adhesion that leads to the development of biofilms occurring in such infections. It was recently demonstrated that Zn-induced B-repeat assembly leads to formation of functional amyloid fibrils, which offer strength and stability to the biofilm.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!