Complex RNA Chain Elongation Kinetics by Wheat Germ RNA Polymerase II

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1984 Apr 11

PMID 6201828

Citations 6

Authors

D Job

R Durand

C Job

M Teissere

Affiliations

Soon will be listed here.

Abstract

Kinetics of RNA chain elongation catalyzed by wheat germ RNA polymerase II have been studied using various synthetic DNA templates in the presence of excess dinucleotide monophosphate primers. With single- or double-stranded homopolymer templates, the double reciprocal plots 1/(velocity) as a function of 1/(nucleotide substrate) exhibit positive, negative or no curvature. With poly(dAT) as template, the mechanism of nucleoside monophosphate incorporation into RNA is not the ping-pong kinetic mechanism which was derived for E. coli RNA polymerase (6). Noncomplementary nucleoside triphosphates inhibit RNA transcription allosterically. Cordycepin triphosphate behaves as ATP, and not only inhibits AMP incorporation but also that of UMP and GMP on appropriate templates. The reason for this complex kinetic behavior is not yet understood. Possibilities are raised that there are several nucleoside triphosphate binding sites on wheat germ RNA polymerase II, that additional nucleoside triphosphate dependent enzymatic activities are required for reaction to occur or that the Km value for incorporation of a given nucleoside monophosphate into RNA is dependent on the length of the RNA chain and/or the nucleotide sequence surrounding the complementary base on the DNA template.

Citing Articles

Base-pair-resolution genome-wide mapping of active RNA polymerases using precision nuclear run-on (PRO-seq).

Mahat D, Kwak H, Booth G, Jonkers I, Danko C, Patel R Nat Protoc. 2016; 11(8):1455-76.

PMID: 27442863 PMC: 5502525. DOI: 10.1038/nprot.2016.086.

Enzymatic properties of plant RNA polymerases : An approach to the study of transcription in plants.

Cooke R, Durand R, Job C, Penon P, Teissere M, Job D Plant Mol Biol. 2013; 3(4):217-25.

PMID: 24310433 DOI: 10.1007/BF00029657.

Effect of low nucleotide concentrations on abortive elongation catalysed by wheat-germ RNA polymerase II.

Job C, Dietrich J, Shire D, Teissere M, Job D Biochem J. 1987; 244(1):151-7.

PMID: 3499138 PMC: 1147966. DOI: 10.1042/bj2440151.

Kinetic co-operativity of wheat-germ RNA polymerase II with adenosine 5'-[beta gamma-imido]triphosphate as substrate.

Job C, Soulie J, Job D Biochem J. 1988; 252(1):55-63.

PMID: 3421909 PMC: 1149106. DOI: 10.1042/bj2520055.

Effect of Sarkosyl and heparin on single-step addition reactions catalysed by wheat-germ RNA polymerase II--poly[d(A-T)]transcription complexes.

De Mercoyrol L, Job C, Job D Biochem J. 1989; 260(3):795-801.

PMID: 2475103 PMC: 1138747. DOI: 10.1042/bj2600795.

References

Anthony D, GOLDTHWAIT D, Wu C . Studies with the ribonucleic acid polymerase. II. Kinetic aspects of initiation and polymerization. Biochemistry. 1969; 8(1):246-56. DOI: 10.1021/bi00829a035. View

Niyogi S, Stevens A . STUDIES OF THE RIBONUCLEIC ACID POLYMERASE FROM ESCHERICHIA COLI. 3. STUDIES WITH SYNTHETIC POLYRIBONUCLEOTIDES AS TEMPLATES. J Biol Chem. 1965; 240:2587-92. View

Downey K, Jurmark B, So A . Determination of nucleotide sequences at promoter regions by the use of dinucleotides. Biochemistry. 1971; 10(26):4970-5. DOI: 10.1021/bi00802a021. View

Rhodes G, CHAMBERLIN M . Ribonucleic acid chain elongation by Escherichia coli ribonucleic acid polymerase. I. Isolation of ternary complexes and the kinetics of elongation. J Biol Chem. 1974; 249(20):6675-83. View

McClure W, Jovin T . The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. J Biol Chem. 1975; 250(11):4073-80. View

Ninio J, Bernardi F, Brun G, Assairi L, Lauber M, Chapeville F . On the mechanism of nucleotide incorporation into DNA and RNA. FEBS Lett. 1975; 57(2):139-44. DOI: 10.1016/0014-5793(75)80702-2. View

Jendrisak J, Burgess R . A new method for the large-scale purification of wheat germ DNA-dependent RNA polymerase II. Biochemistry. 1975; 14(21):4639-45. DOI: 10.1021/bi00692a012. View

Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View

Sasaki Y, Goto H, Ohta H, Kamikubo T . Template activity of synthetic deoxyribonucleotide polymers in the eukaryotic DNA-dependent RNA polymerase reaction. Eur J Biochem. 1976; 70(2):369-75. DOI: 10.1111/j.1432-1033.1976.tb11026.x. View

10.

Volloch V, Rits S, TUMERMAN L . A possible mechanism responsible for the correction of transcription errors. Nucleic Acids Res. 1979; 6(4):1535-46. PMC: 327788. DOI: 10.1093/nar/6.4.1535. View

11.

Nierman W, CHAMBERLIN M . Studies of RNA chain initiation by Escherichia coli RNA polymerase bound to T7 DNA. Direct analysis of the kinetics and extent of RNA chain initiation at T7 promoter A1. J Biol Chem. 1979; 254(16):7921-6. View

12.

Shaw P, Saunders G . Stimulation of RNA synthesis by dinucleotides with eukaryotic RNA polymerase. FEBS Lett. 1979; 106(1):104-10. DOI: 10.1016/0014-5793(79)80704-8. View

13.

Shimamoto N, Wu C . Mechanism of ribonucleic acid chain initiation. 2. A real time analysis of initiation by the rapid kinetic technique. Biochemistry. 1980; 19(5):849-56. DOI: 10.1021/bi00546a004. View

14.

Grossmann K, Seitz U . RNA polymerase I from higher plants. Evidence for allosteric regulation and interaction with a nuclear phosphatase activity controlled NTP pool. Nucleic Acids Res. 1979; 7(7):2015-29. PMC: 342363. DOI: 10.1093/nar/7.7.2015. View

15.

Nierman W, CHAMBERLIN M . The effect of low substrate concentrations on the extent of productive RNA chain initiation from T7 promoters A1 and A2 by Escherichia coli RNA polymerase. J Biol Chem. 1980; 255(10):4495-500. View

16.

Shaw P, Marshall M, Saunders G . Dinucleotide priming of RNA synthesis. Cytogenet Cell Genet. 1980; 26(2-4):211-22. DOI: 10.1159/000131442. View

17.

Grossmann K, Seitz H . Cooperative effects of RNA polymerase from higher plant cells and Escherichia coli: a comparison. FEBS Lett. 1980; 116(2):193-5. DOI: 10.1016/0014-5793(80)80641-7. View

18.

Lescure B, Williamson V, Sentenac A . Efficient and selective initiation by yeast RNA polymerase B in a dinucleotide-primed reaction. Nucleic Acids Res. 1981; 9(1):31-45. PMC: 326666. DOI: 10.1093/nar/9.1.31. View

19.

Dennis D, Sylvester J . RNA polymerase: a model for rotational translocation. FEBS Lett. 1981; 124(2):135-9. DOI: 10.1016/0014-5793(81)80121-4. View

20.

Rackwitz H, Rohde W, Sanger H . DNA-dependent RNA polymerase II of plant origin transcribes viroid RNA into full-length copies. Nature. 1981; 291(5813):297-301. DOI: 10.1038/291297a0. View