Viroid RNA is accepted as a template for in vitro transcription by DNA-dependent DNA polymerase I and RNA polymerase from Escherichia coli

1982 ◽  
Vol 2 (11) ◽  
pp. 929-939 ◽  
Author(s):  
Wolfgang Rohde ◽  
Hans-Richard Rackwitz ◽  
Frank Boege ◽  
Heinz L. Sänger
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Dna Polymerase ◽  
Unit Length ◽  
Dna Polymerase I ◽  
Experimental Conditions ◽  
In Vitro Synthesis ◽  
Polymerase I

The RNA genome of potato spindle tuber viroid (PSTV) is transcribed in vitro into complementary DNA and RNA by DNA-dependent DNA polymerase I and RNA polymerase, respectively, from Escherichia coli. In vitro synthesis of complementary RNA produces distinct transcripts larger than unit length thus reflecting the in vivo mechanism of viroid replication. The influence of varying experimental conditions on the transcription process is studied; actinomycin D is found to drastically reduce complementary RNA synthesis from the PSTV RNA template by RNA polymerase.

Effect of caffeine on DNA polymerase I from Escherichia coli studies in vitro and in vivo

1978 ◽  
Vol 51 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Knut A. Solberg ◽  
Steinar Øvrebø ◽  
Ruth K. Kleppe ◽  
Kjell Kleppe
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Dna Polymerase I ◽  
Polymerase I

DNA polymerase I proofreading exonuclease activity is required for endonuclease V repair pathway both in vitro and in vivo

DNA Repair ◽  
2018 ◽  
Vol 64 ◽  
pp. 59-67 ◽  
Author(s):  
Kang-Yi Su ◽  
Liang-In Lin ◽  
Steven D. Goodman ◽  
Rong-Syuan Yen ◽  
Cho-Yuan Wu ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Exonuclease Activity ◽  
Repair Pathway ◽  
Dna Polymerase I ◽  
Endonuclease V ◽  
Polymerase I

Cis-syn thymine dimers are not absolute blocks to replication by DNA polymerase I of Escherichia coli in vitro

Biochemistry ◽  
1990 ◽  
Vol 29 (6) ◽  
pp. 1624-1632 ◽  
Author(s):  
John Stephen Taylor ◽  
Christine L. O'Day
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Dna Polymerase I ◽  
Thymine Dimers ◽  
Polymerase I

Caffeine inhibits DNA polymerase I from Escherichia coli: studies in vitro

1982 ◽  
Vol 3 (2) ◽  
pp. 151-153 ◽  
Author(s):  
R. Balachandran ◽  
A. Srinivasan
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Dna Polymerase I ◽  
Polymerase I

Biochemical characterization of human DNA polymerase i provides clues to its biological function

2001 ◽  
Vol 29 (2) ◽  
pp. 183-187 ◽  
Author(s):  
A. Tissier ◽  
E. G. Frank ◽  
J. P. McDonald ◽  
A. Vaisman ◽  
A. R. Fernàndez deHenestrosa Henestrosa ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Biochemical Characterization ◽  
Short Review ◽  
Biochemical Properties ◽  
Dna Polymerase I ◽  
Polymerase I

The human RAD30B gene has recently been shown to encode a novel DNA polymerase, DNA polymerase i (poli). The role of poli within the cell is presently unknown, and the only clues to its cellular function come from its biochemical characterization in vitro. The aim of this short review is, therefore, to summarize the known enzymic activities of poli and to speculate as to how these biochemical properties might relate to its in vivo function.

scholarly journals Role of Escherichia coli DNA Polymerase I in Conferring Viability upon the dnaN159 Mutant Strain

2007 ◽  
Vol 189 (13) ◽  
pp. 4688-4695 ◽  
Author(s):  
Robert W. Maul ◽  
Laurie H. Sanders ◽  
James B. Lim ◽  
Rosemary Benitez ◽  
Mark D. Sutton
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Temperature Sensitive ◽  
Mutant Form ◽  
Sliding Clamp ◽  
Pol I ◽  
Pol Iii ◽  
Polymerase I

ABSTRACT The Escherichia coli dnaN159 allele encodes a mutant form of the β-sliding clamp (β159) that is impaired for interaction with the replicative DNA polymerase (Pol), Pol III. In addition, strains bearing the dnaN159 allele require functional Pol I for viability. We have utilized a combination of genetic and biochemical approaches to characterize the role(s) played by Pol I in the dnaN159 strain. Our findings indicate that elevated levels of Pol I partially suppress the temperature-sensitive growth phenotype of the dnaN159 strain. In addition, we demonstrate that the β clamp stimulates the processivity of Pol I in vitro and that β159 is impaired for this activity. The reduced ability of β159 to stimulate Pol I in vitro correlates with our finding that single-stranded DNA (ssDNA) gap repair is impaired in the dnaN159 strain. Taken together, these results suggest that (i) the β clamp-Pol I interaction may be important for proper Pol I function in vivo and (ii) in the absence of Pol I, ssDNA gaps may persist in the dnaN159 strain, leading to lethality of the dnaN159 ΔpolA strain.

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