scholarly journals Relationship between RNA polymerase I activity and ornithine decarboxylase in rat liver tissues

1987 ◽  
Vol 241 (1) ◽  
pp. 169-174 ◽  
Author(s):  
M Urata ◽  
N Suzuki ◽  
T Hosoya
Keyword(s):  
Rna Polymerase ◽  
Ornithine Decarboxylase ◽  
Rat Liver ◽  
Protein Sequence ◽  
Rna Polymerase I ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Polymerase I ◽  
The Relationship ◽  
Liver Tissues

In order to examine the relationship between RNA polymerase I and ornithine decarboxylase (ODC), three lines of experiments were performed, with the following results. The glucocorticoid-induced increase of RNA polymerase I in rat liver nuclei was not abolished by administration of inhibitors of ODC synthesis and activity, namely 1,3-diaminopropane and 2-difluoromethylornithine respectively. Anti-ODC antibody did not cross-react with RNA polymerase I solubilized from rat liver nucleoli, indicating the absence of a common protein sequence in these enzymes. The ODC preparation which was treated with transglutaminase in the presence of putrescine could not stimulate the activity of RNA polymerase I in nuclei of liver and prostate. All these results suggest that the increases in ODC protein or activity are not a prerequisite to the increase in RNA polymerase I after hormonal or physiological stimuli, but rather that the increases in both enzymes are separate responses to the primary stimuli.

REGULATION OF DNA-DEPENDENT: RNA POLYMERASE I ACTIVITY IN RAT LIVER NUCLEI

1978 ◽  
pp. 525
Author(s):  
John A. Todhunter ◽  
Michael Tainsky ◽  
Herbert Weissbach ◽  
Nathan Brot
Keyword(s):  
Rna Polymerase ◽  
Rat Liver ◽  
Rna Polymerase I ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Polymerase I

scholarly journals Effects of glucocorticoid and cycloheximide on the activity and amount of RNA polymerase I in nuclei of rat liver

1986 ◽  
Vol 235 (3) ◽  
pp. 699-705 ◽  
Author(s):  
H Matsui ◽  
H Yazawa ◽  
N Suzuki ◽  
T Hosoya
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rat Liver ◽  
Protein S ◽  
Rna Polymerase I ◽  
Free Form ◽  
Precursor Synthesis ◽  
Liver Nuclei ◽  
Polymerase I ◽  
Adrenalectomized Rats

The activity of the template-engaged form of RNA polymerase I from livers of adrenalectomized rats was about 50-60% of that of normal control rats, and increased about 2-fold at 6 h after the administration of dexamethasone. However, no change was found in the activity of the ‘free’ form of RNA polymerase I or the template-engaged form of RNA polymerase II. Immunochemical studies using guinea-pig anti-(RNA polymerase I) serum disclosed that the total number of RNA polymerase I molecules did not vary during the treatment with dexamethasone. Cycloheximide caused a rapid decrease in the template-engaged form of RNA polymerase I activity in normal rats and in dexamethasone-treated (6 h) adrenalectomized rats, to the value in adrenalectomized rats, but affected it only slightly in adrenalectomized rats. The elongation rate of rRNA-precursor synthesis in liver nuclei was not affected by a change in the concentration of circulating dexamethasone. From these results, it is concluded that about half the rRNA-precursor synthesis in rat liver is regulated by glucocorticoids, probably through the synthesis of short-lived protein(s) which may play a role in conversion of the ‘dormant’ form of RNA polymerase I into the ‘engaged’ form.

Stimulation of nuclear RNA polymerase I activity by a soluble factor isolated from young rat liver nuclei

AGE ◽  
1983 ◽  
Vol 6 (4) ◽  
pp. 106-112 ◽  
Author(s):  
Patricia Fitzpatrick-Dimond ◽  
John A. Todhunter ◽  
Sameeh S. Elridi
Keyword(s):  
Rna Polymerase ◽  
Rat Liver ◽  
Rna Polymerase I ◽  
Soluble Factor ◽  
Nuclear Rna ◽  
Liver Nuclei ◽  
Young Rat ◽  
Polymerase I ◽  
Nuclear Rna Polymerase ◽  
Stimulation Of

Relationship of ornithine decarboxylase to RNA polymerase I activity

Life Sciences ◽  
1975 ◽  
Vol 17 (12) ◽  
pp. 1769-1775 ◽  
Author(s):  
Carol-Ann Manen ◽  
Diane H. Russell
Keyword(s):  
Rna Polymerase ◽  
Ornithine Decarboxylase ◽  
Rna Polymerase I ◽  
Polymerase I ◽  
Relationship Of

Alterations in DNA-dependent RNA polymerase I from rat liver accompanying ethionine administration

1982 ◽  
Vol 105 (3) ◽  
pp. 799-805 ◽  
Author(s):  
Haruko Yamano ◽  
Yasuko Sawai ◽  
Wen Long Thung ◽  
Fumiyasu Sato ◽  
Kinji Tsukada
Keyword(s):  
Rna Polymerase ◽  
Rat Liver ◽  
Rna Polymerase I ◽  
Polymerase I

Inactivation of rat liver RNA polymerases I and II and yeast RNA polymerase I by pyridoxal 5'-phosphate. Evidence for the participation of lysyl residues at the active site

Biochemistry ◽  
1975 ◽  
Vol 14 (22) ◽  
pp. 4907-4911 ◽  
Author(s):  
Joseph Martial ◽  
Josefina Zaldivar ◽  
Paulina Bull ◽  
Alejandro Venegas ◽  
Pablo Valenzuela
Keyword(s):  
Rna Polymerase ◽  
Rat Liver ◽  
Active Site ◽  
Rna Polymerases ◽  
Rna Polymerase I ◽  
Polymerase I

scholarly journals The relationship between the activity of DNA-dependent RNA polymerase I and the rate of synthesis of rRNA in hepatoma cells in culture

1981 ◽  
Vol 194 (1) ◽  
pp. 43-51 ◽  
Author(s):  
E A Thompson ◽  
R H Keith ◽  
A H Cavanaugh ◽  
K M Wood
Keyword(s):  
Steady State ◽  
Rna Polymerase ◽  
Cell Lines ◽  
Rna Polymerase I ◽  
28S Rrna ◽  
Pol I ◽  
Cell Enzyme ◽  
Ribonucleoside Triphosphate ◽  
Polymerase I ◽  
The Relationship

Cell culture lines were established from the transplantable mouse hepatomas H6 and H129. Both cell lines had a doubling time about 30 h when maintained in medium containing 5% foetal bovine serum. H6 cells contained about 3-4 times more DNA-dependent RNA polymerase I (Pol I; ribonucleoside triphosphate–RNA nucleotidyltransferase, EC 2.7.7.6) than did H129 cells. Moreover, the H6-cell enzyme was more heat-labile than that from H129 cells. Steady-state contents of 28S rRNA were measured in both cell lines. Exponentially growing cultures of H6 cells contained about 6.5pg of 28S rRNA/cell, and similar cultures of H129 cells contained about 5.8pg/cell. Stationary cultures of both cell lines contained about 2pg of 28S rRNA/cell. By two different techniques, the half-time for turnover of 28S rRNA was estimated to be 16-17h for both H6 and H129 cells. Knowing the turnover rate and the steady-state concentration, one may calculate that both H6 and H129 cells synthesize 28S rRNA at a rate of about 0.25 pg/h per cell. The amount of template-bound Pol I activity was similar in nuclei isolated from H6 and H129 cell cultures. These data indicate that, although H6 cells contained 3-4 times more Pol I than did H129 cells, both cell lines synthesized rRNA at about the same rate.

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