Nudease-hypersensitive sites in the chromalin domain of the chicken lysozyme gene

Fritton, Hans P.; Sippel, Albrecht E.; Igo‐Kemenes, Tibor

doi:10.1093/nar/11.11.3467

Cited by 115 publications

(83 citation statements)

References 41 publications

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“…Nuclei of HeLa cells were prepared as described previously (14). The DNA concentration in the nuclei suspension was determined by measuring the UV absorption at 260 nm in a 2 M NaCl solution.…”

Section: Methodsmentioning

confidence: 99%

Mitotic Phosphorylation of Histone H3: Spatio-Temporal Regulation by Mammalian Aurora Kinases

Crosio

Fimia

Loury

et al. 2002

Molecular and Cellular Biology

602

468

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Phosphorylation at a highly conserved serine residue (Ser-10) in the histone H3 tail is considered to be a crucial event for the onset of mitosis. This modification appears early in the G 2 phase within pericentromeric heterochromatin and spreads in an ordered fashion coincident with mitotic chromosome condensation. Mutation of Ser-10 is essential in Tetrahymena, since it results in abnormal chromosome segregation and extensive chromosome loss during mitosis and meiosis, establishing a strong link between signaling and chromosome dynamics. Although mitotic H3 phosphorylation has been long recognized, the transduction routes and the identity of the protein kinases involved have been elusive. Here we show that the expression of Aurora-A and Aurora-B, two kinases of the Aurora/AIK family, is tightly coordinated with H3 phosphorylation during the G 2 /M transition. During the G 2 phase, the Aurora-A kinase is coexpressed while the Aurora-B kinase colocalizes with phosphorylated histone H3. At prophase and metaphase, Aurora-A is highly localized in the centrosomic region and in the spindle poles while Aurora-B is present in the centromeric region concurrent with H3 phosphorylation, to then translocate by cytokinesis to the midbody region. Both Aurora-A and Aurora-B proteins physically interact with the H3 tail and efficiently phosphorylate Ser10 both in vitro and in vivo, even if Aurora-A appears to be a better H3 kinase than Aurora-B. Since Aurora-A and Aurora-B are known to be overexpressed in a variety of human cancers, our findings provide an attractive link between cell transformation, chromatin modifications and a specific kinase system.

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Section: Methodsmentioning

confidence: 99%

Mitotic Phosphorylation of Histone H3: Spatio-Temporal Regulation by Mammalian Aurora Kinases

Crosio

Fimia

Loury

et al. 2002

Molecular and Cellular Biology

602

468

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“…Nuclei were isolated from tissues combined from six BALB/c mice, as described by Fritton et al (1980); extracts were pre pared according to Dignam et al (1983). Nuclear proteins were concentrated at 4°C by adding (NFl4)2S04 slowly to 0.3 g/ml, stirring for 1 hr, and pelleting the precipitate at 10,000 rpm in an SS34 rotor for 20 min.…”

Section: Preparation Of Nuclear Extractsmentioning

confidence: 99%

The mouse albumin promoter and a distal upstream site are simultaneously DNase I hypersensitive in liver chromatin and bind similar liver-abundant factors in vitro.

Liu¹,

Bergman²,

Zaret³

1988

Genes Dev.

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In this paper we characterize the chromatin structure and nuclear proteins associated with different transcriptional states of the mouse serum albumin gene. We found the albumin gene to be transcribed in liver at rates 1000-fold or greater than in other tissues tested. We discovered seven DNase I hypersensitive sites encompassing the albumin gene only in liver chromatin, with strong hypersensitivity at the promoter and the enhancer, which is over 10 kb upstream. Using a gel retardation assay, we found a liver nuclear protein, or set of proteins, which binds specifically to DNA of a liver-specific hypersensitive site that maps 3.5 kb upstream, between the promoter and enhancer. Footprinting, heat insensitivity, and binding competition experiments indicate that the protein(s) have characteristics similar to a heat-stable, liver-abundant protein that binds to the albumin promoter and other enhancer and promoter sequences. Finally, we asked whether the liver-specific factors that cause DNase I hypersensitivity in vivo are present concurrently at the various sites in chromatin. We devised a simple new method to reveal that in liver, individual albumin genes are hypersensitive simultaneously at the promoter, the enhancer, and the -3.5-kb site. Thus, transcriptionally active albumin genes appear to contain tissue-abundant factors that are present at three widely spaced points in chromatin, yet at the same point in time. Similar factors binding simultaneously to at least two of these sites could create a specific structure in chromatin required for high-level albumin gene transcription.

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“…These nuclease hypersensitive sites may represent nucleosome-free gaps up to 200 bp in length which facilitate interaction with the transcription machinery (6,18,19,20). Hypersensitive sites associated with transcription are often found considerable distances upstream of the cap site (15,16,21,22). Enhancer elements also exhibit DNase I hypersensitivity at or near them.…”

Section: Introductionmentioning

confidence: 99%

Hypersensitive sites in the 5′ and 3′ flanking regions of the cysteine proteinase I gene ofDictyostelium discoideum

1986

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Nudease-hypersensitive sites in the chromalin domain of the chicken lysozyme gene

Cited by 115 publications

References 41 publications

Mitotic Phosphorylation of Histone H3: Spatio-Temporal Regulation by Mammalian Aurora Kinases

Mitotic Phosphorylation of Histone H3: Spatio-Temporal Regulation by Mammalian Aurora Kinases

The mouse albumin promoter and a distal upstream site are simultaneously DNase I hypersensitive in liver chromatin and bind similar liver-abundant factors in vitro.

Hypersensitive sites in the 5′ and 3′ flanking regions of the cysteine proteinase I gene ofDictyostelium discoideum

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