Results 11 to 20 of about 92,482 (260)

Interaction of Non-histone Chromosomal Proteins HMG1 and HMG2 with DNA [PDF]

open access: yesEuropean Journal of Biochemistry, 1977
Interaction between non-histone protein HMG1 or HMG2 and DNA has been studied by using thermal denaturation and circular dichroism (CD) spectroscopy. We have made the following observations. 1. The binding of each of these two proteins to DNA stabilizes the latter, as shown by an increase in melting temperature of 20 degrees C (from 45 degrees C to ...
Hsueh Jei Li   +3 more
openaire   +4 more sources

Conformational Studies of Two Non‐histone Chromosomal Proteins and Their Interactions with DNA [PDF]

open access: yesEuropean Journal of Biochemistry, 1976
The conformational properties of two non-histone chromosomal proteins (high-mobility-group proteins 1 and 2) have been studied by spectroscopic methods. The interaction of high-mobility-group protein 1 with DNA has also been studied. 1. Circular dichroism results indicate that in the presence of salt both proteins are 40-50% helical between pH 1 and 9.
Peter D. Cary   +5 more
openaire   +4 more sources

Non‐histone Chromosomal Proteins [PDF]

open access: yesEuropean Journal of Biochemistry, 1975
We describe a method for fractionation of chromatin components by selective dissociation with salt in buffers containing 5 M urea in combination with chromatography on hydroxyapatite at 4 °C. This results in two histone and four non‐histone fractions which are recovered in high yield and with minimal proteolytic contamination.Template capacity ...
Horst Blüthmann   +2 more
openaire   +4 more sources

The Similarity between the Primary Structures of Two Non‐histone Chromosomal Proteins [PDF]

open access: yesEuropean Journal of Biochemistry, 1976
A comparison has been made of two non‐histone chromosomal proteins, high‐mobility‐group proteins 1 and 2. Peptides produced from the two proteins by various chemical and enzymic cleavages have been compared by polyacrylamide gel electrophoresis and peptide mapping.
Graham H. Goodwin   +2 more
openaire   +4 more sources

Effect of non-histone chromosomal proteins on transcription in vitro in sea-urchin [PDF]

open access: yesBiochemical Journal, 1978
Non-histone chromosomal proteins prepared from chromosomal material of the sea-urchin Paracentrotus lividus affect RNA synthesis in vitro. 1. The extent of transcription can be radically changed from inhibition to stimulation, depending on the DNA/non-histone chromosomal proteins ratio. 2. A correlation exists between stage of development and influence
E Di Mauro, Francesco Pedone, M. Pomponi
openaire   +4 more sources

The primary structures of non‐histone chromosomal proteins HMG 1 and 2 [PDF]

open access: yesFEBS Letters, 1980
Keith Gooderham   +4 more
openaire   +4 more sources

SUMO control of centromere homeostasis

open access: yesFrontiers in Cell and Developmental Biology, 2023
Centromeres are unique chromosomal loci that form the anchorage point for the mitotic spindle during mitosis and meiosis. Their position and function are specified by a unique chromatin domain featuring the histone H3 variant CENP-A.
Sebastiaan J. W. van den Berg   +2 more
doaj   +1 more source

Selfish chromosomal drive shapes recent centromeric histone evolution in monkeyflowers.

open access: yesPLoS Genetics, 2021
Centromeres are essential mediators of chromosomal segregation, but both centromeric DNA sequences and associated kinetochore proteins are paradoxically diverse across species.
Findley R Finseth   +2 more
doaj   +1 more source

The DNA intercalators ethidium bromide and propidium iodide also bind to core histones

open access: yesFEBS Open Bio, 2014
Eukaryotic DNA is compacted in the form of chromatin, in a complex with histones and other non-histone proteins. The intimate association of DNA and histones in chromatin raises the possibility that DNA-interactive small molecules may bind to chromatin ...
Amrita Banerjee   +6 more
doaj   +1 more source

Identification of genes encoding zinc finger proteins, non-histone chromosomal HMG protein homologue, and a putative GTP phosphohydrolase in the genome of Chilo iridescent virus.

open access: yesNucleic Acids Research, 1994
Five RNA transcripts of about 1.2 to 1.7 kilobases were mapped to a part of the genome of insect iridescent virus type 6 (Chilo iridescent virus; CIV) between genome coordinates 0.832 and 0.856 within the EcoRI DNA fragment F.
P. Schnitzler   +6 more
semanticscholar   +1 more source

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