Stable DNA-protein complexes in eukaryotic chromatin

Avramova, Zoya; Tsanev, Roumen

doi:10.1016/0022-2836(87)90704-2

Cited by 33 publications

(28 citation statements)

References 11 publications

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“…A number of internal formative elements have already been implicated in the morphological development of spermatozoa, including the characterized stable DNA-protein complexes in the sperm nucleus of rams (Avramova & Tsanev, 1987). DNA-anchoring proteins, located at the implantation fossa of hamster spermatozoa, have also been characterized (Ward & Coffey, 1989).…”

Section: Resultsmentioning

confidence: 99%

Quantitative fluorometry of abnormal mouse sperm nuclei

Pogany¹,

Balhorn²

1992

Reproduction

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Summary. An extensive quantitative analysis of deformed mouse spermatozoa was undertaken. Improvements over previous studies included the isolation and purification of sperm nuclei, a multifaceted analytical approach using several fluorochromes and the analysis of individual nuclei classified into shape categories.Malformed sperm nuclei in BALB/c mice could not be distinguished from normal ones in terms of total and basic proteins, sulfhydryl and disulfide group concentration, DNA concentration and chromatin organization. The shape of sperm nuclei is therefore probably determined by the manner in which the internal biochemical components are assembled.

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Section: Resultsmentioning

confidence: 99%

Quantitative fluorometry of abnormal mouse sperm nuclei

Pogany¹,

Balhorn²

1992

Reproduction

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“…One potential clue is provided by the fact that C1D binds to DNA in an extremely stable fashion, as evidenced by the fact that it remains DNA-associated even after rigorous extraction procedures. Highly stable nonhistone proteins that are bound to DNA tightly have been identified in various systems, including insects, plants, and mammalian cells (Krauth and Werner 1979;Capesius et al 1980;Bodnar et al 1983;Avramova and Tsanev 1987). Although the biological functions for these proteins are still largely obscure, it is noteworthy that some have been reported to be associated with highly repetitive DNA sequences and to be involved in targeting a subset of genomic DNA to the nuclear matrix (Neuer and Werner 1985;NeuerNitsche et al 1988;Werner and Neuer-Nitsche 1989;Pfutz et al 1992).…”

Section: Discussionmentioning

confidence: 99%

DNA end-independent activation of DNA-PK mediated via association with the DNA-binding protein C1D

Yavuzer¹,

Smith²,

Bliss³

et al. 1998

Genes Dev.

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DNA-dependent protein kinase (DNA-PK), which is involved in DNA double-strand break repair and V(D)J recombination, is comprised of a DNA-targeting component termed Ku and an ∼465-kD catalytic subunit, DNA-PK cs . Although DNA-PK phosphorylates proteins in the presence of DSBs or other discontinuities in the DNA double helix in vitro, the possibility exists that it is also activated in other circumstances via its association with additional proteins. Here, through use of the yeast two-hybrid screen, we discover that the recently identified high affinity DNA binding protein C1D interacts with the putative leucine zipper region of DNA-PK cs . Furthermore, we show that C1D can interact with DNA-PK in mammalian cells and that C1D is a very effective DNA-PK substrate in vitro. Finally, we establish that C1D directs the activation of DNA-PK in a manner that does not require DNA termini. Therefore, these studies provide a function for C1D and suggest novel mechanisms for DNA-PK activation in vivo.

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“…RNA was digested with RNase A (50/~g/ml, 1 h, 37 °C) and DNA was precipitated once more with ethanol. The pellet was dissolved in 10 mM Tris buffer pH 7.6, containing 5 mM EDTA, 5 M urea, 1°70 SDS, 0.1°70 2-mercaptoethanol, 2% sarkosyl, and was incubated overnight at 0 ° C. It was then deproteinized either by three extractions with phenol (60°C) and phenol-chloroform-isoamyl alcohol, or by centrifugation in CsCI density gradients (starting density 1.58 g/ml) in the presence of ethidium bromide [3].…”

Section: Isolation Of Plant Nuclei and Deproteinization Of Dnamentioning

confidence: 99%

“…the protein component of the complex survived several cell cycles and was propagated to the daughter cells like DNA [2]. d) This protein component was remarkably similar in both metabolically active and inactive chromatins [2,3] and in chromatins of evolutionary remote eukaryotes -from insects to mammals (results submitted).…”

Section: Introductionmentioning

confidence: 99%

A protein fraction stably linked to DNA in plant chromatin

1988

Self Cite

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DNA from the chromatin of roots and shoots of maize seedlings was isolated and extensively deproteinized by repeated high-salt extractions, by subsequent deproteinizations eliminating noncovalently associated proteins and by CsC1 density gradient centrifugation. Nevertheless, a protein component resisting all extraction procedures was found firmly associated to plant nuclear DNA. This component was responsible for the (125)I uptake when a DNA preparation had been labeled by the chloramine-T method.A residual oligodeoxynucleotide-oligopeptide complex was obtained after extensive digestions of the initial DNA-protein complex with proteases and nucleases. The stability of this complex to different chemical treatments suggested a phosphoester type of a linkage. The hydrolysis of this complex by phosphodiesterases indicated that the protein component was linked to plant chromosomal DNA through a phosphodiester bond formed by a hydroxyaminoacid and a 5'-end DNA phosphate. Two-dimensional tryptic peptide mapping of the proteins isolated from the two maize chromatins revealed a high degree of similarity to the corresponding proteins of animal origin. Its conservative structure suggests an important role for this protein component in the functioning of the eukaryotic genome.

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Stable DNA-protein complexes in eukaryotic chromatin

Cited by 33 publications

References 11 publications

Quantitative fluorometry of abnormal mouse sperm nuclei

Quantitative fluorometry of abnormal mouse sperm nuclei

DNA end-independent activation of DNA-PK mediated via association with the DNA-binding protein C1D

A protein fraction stably linked to DNA in plant chromatin

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