Role of non‐histone components in determining organ specificity of rabbit chromatins

Gilmour, Raymond; Paul, John

doi:10.1016/0014-5793(70)80366-0

Cited by 177 publications

(58 citation statements)

References 5 publications

(3 reference statements)

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“…These proteins possess tissue specificity (10-17) and are capable of interacting with DNA to selectively modify transcription (18,19 Fla. 32601 in the nonhistone proteins have been described in various phases of the HeLa cell cycle (20,22).…”

Section: Introductionmentioning

confidence: 99%

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Role of Nonhistone Chomosomal Proteins in the Restriction of Mitotic Chromatin Template Activity

Stein

Farber

1972

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

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RNA synthesis virtually ceases during mitosis in eukaryotic cells. This phenomenon is explainable, at least in part, by the reduced template activity for RNA synthesis of mitotic chromatin. The restriction in template activity can be accounted for by the presence in the chromatin of mitotic-specific nonhistone proteins. Chromatin reconstituted by gradient dialysis from the pooled histones of S-phase and mitotic chromatin and the nonhistone proteins of mitotic chromatin had a template activity similar to that of native mitotic chromatin, and lower than native S-phase chromatin or chromatin reconstituted with the pooled histones and the S-phase and nonhistone proteins. The template activity was identical for chromatin reconstituted from the pooled nonhistone proteins and either the histones from S-phase or mitotic chromatin. These results are supported with data showing that the procedure of reconstitution produces a chromatin indistinguishable in its protein composition both qualitatively and quantitatively from its native counterpart.Macromolecular metabolism is strikingly altered in eukaryotic cells during mitosis. RNA synthesis virtually ceases (1-4), and the rate of protein synthesis is significantly reduced (3, 5). Johnson and Holland (6) reported that mitotic chromatin has a reduced template activity for RNA synthesis. We recently confirmed this observation and have shown that this restriction of chromatin template activity may be produced by the chromosomal protein fraction specific for mitotic chromatin (7). The template activity of chromatin reconstituted by gradient dialysis from purified HeLa cell DNA and the chromosomal proteins isolated from Colcemidarrested metaphase cells was considerably less than that of chromatin reconstituted from S-phase chromosomal proteins. The degree of template restriction was proportional to the amount of mitotic chromosomal proteins in the reconstituted chromatin. This finding led us to suggest that the inhibition of template activity of mitotic chromatin might be accounted for by a constituent of the chromosomal protein fraction that binds to DNA during mitosis and thereby prevents transcription by RNA polymerase (7).Recent studies from several laboratories have indicated that the nonhistone chromosomal proteins may play a significant role in the control of gene expression in eukaryotic cells (8,9). These proteins possess tissue specificity (10-17) and are capable of interacting with DNA to selectively modify transcription (18,19 Fla. 32601 in the nonhistone proteins have been described in various phases of the HeLa cell cycle (20,22).In this report we show that nonhistone chromosomal proteins may be responsible for the inhibition of template activity of mitotic chromatin. MATERIALS AND METHODSExponentially growing HeLa S3 cells were maintained in suspension culture in Joklik-modified Eagle's Minimal Essential Medium supplemented with 3.5% (each) of calf and fetal-calf serum. Synchronization of the cells was produced (20) by 2 cycles of 2 mM thymidine block...

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Section: Introductionmentioning

confidence: 99%

“…These proteins possess tissue specificity (10)(11)(12)(13)(14)(15)(16)(17) and are capable of interacting with DNA to selectively modify transcription (18,19). In HeLa cells, nonhistone chromosomal proteins are actively synthesized throughout the cell cycle (20), including the mitotic phase (21).…”

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confidence: 99%

Role of Nonhistone Chomosomal Proteins in the Restriction of Mitotic Chromatin Template Activity

Stein

Farber

1972

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

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“…Common to all the models is the supposition that binding involves several different modes of interaction and that for highly specific recognition to occur, a protein has to envelope the DNA in one of its cavities or has to be enveloped by the DNA in one of the grooves. Since non-histone chromosomal proteins are largely regarded as being involved in the regulation of gene expression [21][22][23][24][25] a close fit for their binding to DNA is required. Intercalating agents are therefore likely to interfere with their binding.…”

Section: Discussionmentioning

confidence: 99%

Binding and arrangement of non‐histone proteins in chromatin‐like structures from mammalian cells

Jost

Clark

1975

FEBS Letters

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“…We have found some modifications of the 3H/14C ratio in several fractions, the synthesis of some of the acidic proteins is increased (fraction 8), while the synthesis of some others is decreased (fraction 16), in regenerating liver. After hepatectomy, as during rapid cell proliferation, there is an increase in the synthesis of RNA and of the bulk of the acidic proteins [21,24,251 . These observations favour a nuclear control of the repair mechanism after hepatectomy.…”

Section: Comparison Of' the Turnover Ratesmentioning

confidence: 99%

Synthesis and turnover of liver chromatin acidic proteins

Dastugue¹,

Hanoune²,

Kruh³

1971

FEBS Letters

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Role of non‐histone components in determining organ specificity of rabbit chromatins

Cited by 177 publications

References 5 publications

Role of Nonhistone Chomosomal Proteins in the Restriction of Mitotic Chromatin Template Activity

Role of Nonhistone Chomosomal Proteins in the Restriction of Mitotic Chromatin Template Activity

Binding and arrangement of non‐histone proteins in chromatin‐like structures from mammalian cells

Synthesis and turnover of liver chromatin acidic proteins

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