Kinetic analysis of nucleolar rna polymerase I in diploid and phylogenetically tetraploid fish species

1984 ◽  
Vol 77 (3) ◽  
pp. 483-491
Author(s):  
M. Leipoldt ◽  
A. Ebrecht
Keyword(s):  
Rna Polymerase ◽  
Kinetic Analysis ◽  
Fish Species ◽  
Rna Polymerase I ◽  
Polymerase I ◽  
Nucleolar Rna

scholarly journals Transient-State Kinetic Analysis of the RNA Polymerase I Nucleotide Incorporation Mechanism

2015 ◽  
Vol 109 (11) ◽  
pp. 2382-2393 ◽  
Author(s):  
Francis D. Appling ◽  
Aaron L. Lucius ◽  
David A. Schneider
Keyword(s):  
Rna Polymerase ◽  
Kinetic Analysis ◽  
Transient State ◽  
Rna Polymerase I ◽  
Nucleotide Incorporation ◽  
Polymerase I ◽  
State Kinetic

scholarly journals High concentration of RNA polymerase I is responsible for the high rate of nucleolar transcription

1980 ◽  
Vol 188 (2) ◽  
pp. 381-385 ◽  
Author(s):  
F L Yu
Keyword(s):  
Rna Polymerase ◽  
Rna Synthesis ◽  
Rna Polymerases ◽  
Rna Polymerase I ◽  
High Rate ◽  
Unit Weight ◽  
High Concentration ◽  
Steady State Condition ◽  
Polymerase I ◽  
Nucleolar Rna

When isolated rat liver nuclei and nucleoli are compared for RNA synthesis in vitro, the rate of nucleolar RNA synthesis is found to be more than 10 times higher. In order to understand this high rate of nucleolar transcription, DNA from both nuclear and nucleolar fractions was isolated and compared for the ability to direct RNA synthesis with homologous RNA polymerases. No difference between these two templates is evident. On the other hand, when the total nuclear and nucleolar RNA polymerases are isolated and compared on a per-unit-weight-of-DNA basis, it becomes clear that the nucleolus has a 10-fold higher RNA polymerase concentration than the nucleus. This result suggests that RNA polymerase I concentration rather than the nucleolar DNA template efficiency is responsible for the observed high rate of nucleolar transcription under the normal steady-state condition.

scholarly journals Purification and properties of a nuclear protein kinase associated with ribonucleic acid polymerase I

1978 ◽  
Vol 169 (2) ◽  
pp. 355-359 ◽  
Author(s):  
J Hirsch ◽  
O J Martelo
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Rna Polymerase ◽  
Nuclear Protein ◽  
Catalytic Properties ◽  
Rna Polymerase I ◽  
Purification And Properties ◽  
Enzyme Subunits ◽  
Polymerase I ◽  
Nucleolar Rna

A cyclic AMP-dependent nuclear protein kinase was found to be closely associated with rat liver nucleolar RNA polymerase I throughout most of its purification. This protein kinase was purified to near homogeneity. It exhibits a number of unusual catalytic properties, including the inability to utilize Mn2+ when RNA polymerase is the substrate and the ability to phosphorylate both acidic and basic substrates. Phosphorylation of RNA polymerase I by this protein kinase results in the formation of phosphoester bonds characteristic of phosphoserine and phosphothreonine. Radioautography of polyacrylamide-gel electrophoretograms of the phosphorylated RNA polymerase I revealed that the 32P was located primarily on enzyme subunits SA1, SA3, SA5, and SA6 [nomenclature of Kedinger, Gissinger & Chambon (1974) Eur. J. Biochem, 44, 421-436].

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