The effect of estradiol injections upon chicken liver nuclei ribonucleic acid polymerase

Weill, J; Busch, S.; Chambon, Pierre; Mandel, P.

doi:10.1016/0006-291x(63)90036-6

Cited by 37 publications

(10 citation statements)

References 4 publications

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“…Over 40 years ago, P. Chambon and colleagues discovered that the addition of NAD to hen liver nuclear extracts stimulated the synthesis of poly-ADP-ribose (65,433), paving the way for research into the biology of mono-and poly-ADPribose. A landmark meeting on ADP-ribosylation reactions, held in October 2005 in Newcastle, United Kingdom, commemorated this important scientific anniversary.…”

Section: Introductionmentioning

confidence: 99%

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Hassa

Haenni

Elser

et al. 2006

Microbiol Mol Biol Rev

635

644

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SUMMARY Since poly-ADP ribose was discovered over 40 years ago, there has been significant progress in research into the biology of mono- and poly-ADP-ribosylation reactions. During the last decade, it became clear that ADP-ribosylation reactions play important roles in a wide range of physiological and pathophysiological processes, including inter- and intracellular signaling, transcriptional regulation, DNA repair pathways and maintenance of genomic stability, telomere dynamics, cell differentiation and proliferation, and necrosis and apoptosis. ADP-ribosylation reactions are phylogenetically ancient and can be classified into four major groups: mono-ADP-ribosylation, poly-ADP-ribosylation, ADP-ribose cyclization, and formation of O-acetyl-ADP-ribose. In the human genome, more than 30 different genes coding for enzymes associated with distinct ADP-ribosylation activities have been identified. This review highlights the recent advances in the rapidly growing field of nuclear mono-ADP-ribosylation and poly-ADP-ribosylation reactions and the distinct ADP-ribosylating enzyme families involved in these processes, including the proposed family of novel poly-ADP-ribose polymerase-like mono-ADP-ribose transferases and the potential mono-ADP-ribosylation activities of the sirtuin family of NAD+-dependent histone deacetylases. A special focus is placed on the known roles of distinct mono- and poly-ADP-ribosylation reactions in physiological processes, such as mitosis, cellular differentiation and proliferation, telomere dynamics, and aging, as well as “programmed necrosis” (i.e., high-mobility-group protein B1 release) and apoptosis (i.e., apoptosis-inducing factor shuttling). The proposed molecular mechanisms involved in these processes, such as signaling, chromatin modification (i.e., “histone code”), and remodeling of chromatin structure (i.e., DNA damage response, transcriptional regulation, and insulator function), are described. A potential cross talk between nuclear ADP-ribosylation processes and other NAD+-dependent pathways is discussed.

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Section: Introductionmentioning

confidence: 99%

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Hassa

Haenni

Elser

et al. 2006

Microbiol Mol Biol Rev

635

644

View full text Add to dashboard Cite

show abstract

“…There have been over 40 years of research into the biology of protein ADP‐ribosylation (Chambon et al , 1963; Weill et al , 1963) and in vivo evidence suggests that this post‐translational modification is important in gene expression. In particular, this occurs through the regulation of both chromatin structure and transcription in the nuclei of metazoan cells.…”

Section: Introductionmentioning

confidence: 99%

The macro domain is an ADP-ribose binding module

Karras

Kustatscher

Buhecha

et al. 2005

EMBO J

455

504

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The ADP-ribosylation of proteins is an important posttranslational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long-term memory formation. Yet no protein modules are known that specifically recognize the ADP-ribose nucleotide. We provide biochemical and structural evidence that macro domains are high-affinity ADP-ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP-ribose. In addition, some macro domain proteins also recognize poly-ADP-ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP-ribose.

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“…Recent evidence from several Laboratories suggests that the activity of DNA-dependent RNA polymerase in isolated nuclei reflects the growth rate of the tissue (Hancock, Zelis, Shaw & Williams-Ashman, 1962;Weill, Busch, Chambon & Mandel, 1963;Gorski, 1964;Tsukada & Lieberman, 1964;Tata & Widnell, 1966;Pegg & Komer, 1965). Therefore the aims of the present work were, first, to determine whether the administration of growth hormone and testosterone in vivo caused a stimulation of DNA-dependent RNA-polymerase activity in isolated liver nuclei.…”

mentioning

confidence: 99%

Additive effects of thyroid hormone, growth hormone and testosterone on deoxyribonucleic acid-dependent ribonucleic acid polymerase in rat-liver nuclei

Widnell¹,

Tata²

1966

Biochemical Journal

114

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1. The stimulations of DNA-dependent RNA polymerase in isolated rat-liver nuclei by thyroid hormone, human growth hormone and testosterone are compared. 2. Single or multiple administrations of growth-promoting doses of tri-iodo-l-thyronine, human growth hormone and testosterone stimulate the Mg(2+)-activated RNA-polymerase reaction in nuclei from thyroidectomized, hypophysectomized and castrated rats respectively. The magnitude of stimulation was proportional to the degree of enhancement of liver growth by each hormone. After a single injection, the latent period preceding the stimulation was 1, 2 and 10hr. for growth hormone, testosterone and tri-iodothyronine respectively. The time-course of stimulation of enzyme activity and the synthesis of rapidly labelled nuclear RNA in vivo were also different for each hormone. 3. Growth hormone administration failed to stimulate the Mn(2+)/ammonium sulphate-activated RNA-polymerase reaction. Thyroid hormone and testosterone, however, stimulated it but the effect was less pronounced and occurred several hours later than that observed for the Mg(2+)-activated RNA-polymerase reaction. 4. In combination experiments, hypophysectomized or the thyroidectomized rats were given growth hormone or tri-iodothyronine in a single or repeated doses at levels that produced the maximum stimulation of Mg(2+)-activated RNA-polymerase activity. Taking into account the different latent period for each hormone, a single administration of the second hormone caused an additional stimulation of the enzyme activity. Similar additive effects were observed in thyroidectomized-castrated rats after treatment with tri-iodothyronine and testosterone. The magnitude of the additional stimulation caused by the administration of the second hormone was compatible with the capacity of that hormone to promote liver growth in rats deprived of it. 5. It is concluded that, although these hormones have some similar effects, the regulation of nuclear RNA synthesis may be mediated via different routes for each hormone.

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The effect of estradiol injections upon chicken liver nuclei ribonucleic acid polymerase

Cited by 37 publications

References 4 publications

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

The macro domain is an ADP-ribose binding module

Additive effects of thyroid hormone, growth hormone and testosterone on deoxyribonucleic acid-dependent ribonucleic acid polymerase in rat-liver nuclei

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