DOI: 10.1111/j.1432-1033.1975.tb20989.x. RNA Polymerase B from <i>Drosophila melanogaster</i> Larvae

RNA Polymerase B from Drosophila melanogaster Larvae

10.1111/j.1432-1033.1975.tb20989.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

A purification procedure is described by which we obtained DNA‐dependent RNA polyrnerase B (or II) from third‐instar larvae of Drosophila melanogaster in essentially pure form. The enzyme is similar to the analogous polymerases from other eukaryotes in its enzymic and structural properties. lt preferentially transcribes DNAs containing single‐stranded regions, and it is inhibited by low amounts of the toxin α‐amanitin; 50 % inhibition occurs at an α‐amanitin concentration of 0.03 μ/m1. Dodecylsulfate‐polyacrylamide gel electrophoresis resolves the purified Drosophila polymerase B into ten polypeptides with molecular weights as follows: 1 (174000), 2 (137000), 3 (34000). 4 (22000). 5 (18000), 6 and 7 (16000), 8 (15000), and 9 and 10 (less than 15000). The relative amounts of polypeptides 1–4 were constant at molar ratlos of approximately 1:1:1:2 in different preparations of the enzyme, while the amounts of polypeptides 5–10 showed more variation.An antiserum directed against the Drosophila RNA polymerase B inhibited the activity in vitro of the B enzymes from Drosophila, yeast, and calf thymus. However, only the Drosophila enzyme gave a precipitin reaction with the antiserum. When the antiserum was added to Drosophila RNA polymerase B at different stages of the purification, the resulting precipitates were found to contain nearly constant proportions of seven of the ten polypeptides present in the purified enzyme

Bibliography

GREENLEAF, A. L., & BAUTZ, E. K. F. (1975). RNA Polymerase B from Drosophila melanogaster Larvae. European Journal of Biochemistry, 60(1), 169â179. Portico.

Authors 2

Arno L. GREENLEAF (first)
Ekkehard K. F. BAUTZ (additional)

References 26 Referenced 64

{'key': 'e_1_2_3_2_2', 'first-page': '261', 'volume-title': 'The Enzymes', 'author': 'Chambon P.', 'year': '1974'} / The Enzymes by Chambon P. (1974)
10.1016/S0021-9258(19)44470-0 / J. Biol. Chem. by Phillips J. P. (1973)
10.1016/0020-1790(73)90023-1 / Inseet. Biochem. by Natori S. (1973)
10.1016/S0300-9084(74)80140-9
10.1111/j.1432-1033.1972.tb01910.x
10.1111/j.1432-1033.1972.tb01911.x
10.1016/S0076-6879(71)21046-6 / Methods Enzymol. by Krakow J. S. (1971)
10.1016/S0021-9258(18)94333-4
10.1038/227680a0
10.1016/0022-2836(73)90003-X
10.1016/0003-2697(74)90201-2
10.1073/pnas.70.6.1865
10.1111/j.1432-1033.1973.tb02669.x
10.1016/0006-291X(75)90378-2
10.1111/j.1432-1033.1972.tb01912.x
10.1111/j.1432-1033.1973.tb02726.x
10.1016/S0021-9258(18)63520-3
{'key': 'e_1_2_3_19_2', 'first-page': '743', 'volume-title': 'Procedures in Nucleic Acid Research', 'author': 'Bautz E. K. F.', 'year': '1971'} / Procedures in Nucleic Acid Research by Bautz E. K. F. (1971)
10.1016/S0021-9258(19)52451-6
10.1016/S0021-9258(20)79913-8 / J. Biol. Chem. by Dezélée S. (1974)
10.1016/0006-291X(70)91099-5
10.1016/S0021-9258(20)79902-3
10.1111/j.1432-1033.1974.tb03500.x
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10.1073/pnas.72.1.348
Dezélée S.&Wyers F.(1975)Abstr. 10th Meet. Fed. Eur. Biochem. Soe.Paris no. 185.

Dates

Type	When
Created	20 years, 5 months ago (March 3, 2005, 11:20 a.m.)
Deposited	1 year, 9 months ago (Nov. 22, 2023, 4:45 p.m.)
Indexed	1 year, 9 months ago (Nov. 22, 2023, 10:38 p.m.)
Issued	49 years, 9 months ago (Dec. 1, 1975)
Published	49 years, 9 months ago (Dec. 1, 1975)
Published Online	17 years, 2 months ago (June 28, 2008)
Published Print	49 years, 9 months ago (Dec. 1, 1975)

Funders 0

None

BibTeX

@article{GREENLEAF_1975, title={RNA Polymerase B from Drosophila melanogaster Larvae: Purification and Partial Characterization}, volume={60}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1975.tb20989.x}, DOI={10.1111/j.1432-1033.1975.tb20989.x}, number={1}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={GREENLEAF, Arno L. and BAUTZ, Ekkehard K. F.}, year={1975}, month=dec, pages={169–179} }

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