Studies on the degradation of high mobility group non-histone chromosomal proteins

Goodwin, Graham H.; Walker, John M.; Johns, Ernest W.

doi:10.1016/0005-2787(78)90076-x

Cited by 71 publications

(17 citation statements)

References 20 publications

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“…Histones were then purified from co-extracted proteins, in particular HMG proteins, by gel exclusion chromatography on a Bio Gel P 100 column (46,47) and separated into two fractions: (a) main H1 histones and (b) H1°. The purity of the fractions was confirmed by MALDI-TOF mass spectrometry using a Voyager-DE Pro (Applied Biosystems, Framingham, MA), which showed four major peaks with m/z values in the range of 21,186 to 22,496, indicating that the main H1 histone subfraction contained H1.2-H1.5 and a single peak at 20,781 for the H1°subfraction, in close agreement with previously published data (48).…”

Section: Materials and Methods Preparation Of H1 Histonesmentioning

confidence: 99%

Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions

et al. 2004

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Background:Linker histones constitute a family of lysinerich proteins associated with nucleosome core particles and linker DNA in eukaryotic chromatin. In permeabilized cells, they can be extracted from nuclei by using salt concentration in the range of 0.3 to 0.7 M. Although other nuclear proteins are also extracted at 0.7 M salt, the remaining nucleus represents a template that is relatively intact. Methods: A cytochemical method was used to study the affinity of reconstituted linker histones for chromatin in situ in cultured human fibroblasts. We also investigated their ability to condense chromatin by using DNA-specific osmium ammine staining for electron microscopy. Results: Permeabilized and H1-depleted fibroblast nuclei were suitable for the study of linker histone-chromatin

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Section: Materials and Methods Preparation Of H1 Histonesmentioning

confidence: 99%

Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions

et al. 2004

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“…Mammalian cells contain four well-recognized HMG proteins: HMG1, HMG2, HMG14, and HMG17 (2,3). The amino acid sequences of HMG1 and HMG2 have been determined (4)(5)(6), and it is clear that HMG1 and HMG2 are closely related to each other but quite distinct from HMG14 and HMG17 (7,8).…”

mentioning

confidence: 99%

Loss of chromosomal high mobility group proteins HMG1 and HMG2 when mouse neuroblastoma and Friend erythroleukemia cells become committed to differentiation.

Seyedin¹,

Pehrson²,

Cole³

1981

Proc. Natl. Acad. Sci. U.S.A.

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Chromosomal high mobility group (HMG) proteins HMG1 and HMG2 from mouse neuroblastoma cells and Friend erythroleukemic cells were analyzed by acetic acid/urea/ polyacrylamide gel electrophoresis. Compared to rapidly growing cells, levels of HMG1 and HMG2 were decreased in mouse neuroblastoma cells that had been induced to differentiate by serum deprivation. This comparison revealed a reciprocal relationship between these HMG proteins and Hi0, a histone known to be in higher concentrations in nondividing cells. When cell growth was inhibited by means of density inhibition, however, HMG1 and -2 levels were not affected in either HeLa or mouse neuroblastoma cells, even though Hi0 did accumulate. This observation establishes that HMG1 and -2 contents are not correlated with mitotic rate per se. Treatment of mouse neuroblastoma by sodium butyrate, which stops cell division without commitment to differentiation, had no effect on the level of HMG1 and -2. However, the level was decreased by dibutyryl cyclic AMP and dimethyl sulfoxide treatments, which, like serum deprivation, induced irreversible morphological differentiation in the neuroblastoma cells. Moreover, induction of differentiation (hemoglobin synthesis) in Friend erythroleukemic cells by dimethyl sulfoxide showed a decrease in the contents ofHMG1 and -2. These observations suggest that preferential loss ofHMG1 and -2 in mouse neuroblastoma and Friend erythroleukemia cells may be related to commitment of these cells to differentiation.In recent years considerable attention has been focused on a class of nonhistone chromosomal proteins termed the "high mobility group (HMG)" in reference to their electrophoretic mobility at low pH (1). Mammalian cells contain four well-recognized HMG proteins: HMG1, HMG2, HMG14, and HMG17 (2, 3). The amino acid sequences of HMG1 and HMG2 have been determined (4-6), and it is clear that HMG1 and HMG2 are closely related to each other but quite distinct from HMG14 and HMG17 (7,8). The physiological roles ofHMG1 and HMG2 are not known; however, it has been reported that these proteins may be associated with transcriptionally active chromatin (9-11).A recent survey (12) of some rat and chicken tissues revealed that the level of HMG2 was correlated with rates of cellular proliferation. It follows that HMG2 levels are inversely correlated to those ofhistone H10 because the latter is known (13)(14)(15)

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“…First, proteolytic activity of yeast, especially in stationary cells, is very high [22]; this could explain why the CO band is only detectable in growing cells. Second, HMG proteins are very susceptible to proteolytic degradation [23]. Whatever the interpretation, we must emphasize that these results clearly show the existence of HMG proteins in yeast that belong to the HMGl/2 class.…”

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confidence: 72%

On the presence of HMG proteins in yeast

et al. 1986

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Two polypeptides antigenicalIy related to mammalian HMGl/2 have been detected in the yeast Saccharomyces cerevisiae. One exhibits an electrophoretic mobility in the range of mammalian HMGI/Z whereas the second polypeptide corn&rates with yeast HMG S4. Evidence for the presence of HMG14/17 in yeast has not been obtained by immunological or nuclease digestion-based methods, although their presence cannot be excluded.

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Studies on the degradation of high mobility group non-histone chromosomal proteins

Cited by 71 publications

References 20 publications

Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions

Histone H1 and chromatin interactions in human fibroblast nuclei after H1 depletion and reconstitution with H1 subfractions

Loss of chromosomal high mobility group proteins HMG1 and HMG2 when mouse neuroblastoma and Friend erythroleukemia cells become committed to differentiation.

On the presence of HMG proteins in yeast

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