Escherichia coli DNA polymerase II is homologous to α-like DNA polymerases

1991 ◽  
Vol 226-226 (1-2) ◽  
pp. 24-33 ◽  
Author(s):  
Hiroshi Iwasaki ◽  
Yoshizumi Ishino ◽  
Hiroyuki Toh ◽  
Atsuo Nakata ◽  
Hideo Shinagawa
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Dna Polymerases ◽  
Dna Polymerase Ii

scholarly journals A Novel DNA Polymerase Family Found inArchaea

1998 ◽  
Vol 180 (8) ◽  
pp. 2232-2236 ◽  
Author(s):  
Yoshizumi Ishino ◽  
Kayoko Komori ◽  
Isaac K. O. Cann ◽  
Yosuke Koga
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Pyrococcus Furiosus ◽  
Dna Polymerases ◽  
Open Reading Frames ◽  
Gene Products ◽  
Polymerase Gene ◽  
Hyperthermophilic Archaeon ◽  
Dna Polymerase Ii ◽  
Reading Frames

ABSTRACT One of the most puzzling results from the complete genome sequence of the methanogenic archaeon Methanococcus jannaschii was that the organism may have only one DNA polymerase gene. This is because no other DNA polymerase-like open reading frames (ORFs) were found besides one ORF having the typical α-like DNA polymerase (family B). Recently, we identified the genes of DNA polymerase II (the second DNA polymerase) from the hyperthermophilic archaeonPyrococcus furiosus, which has also at least one α-like DNA polymerase (T. Uemori, Y. Sato, I. Kato, H. Doi, and Y. Ishino, Genes Cells 2:499–512, 1997). The genes in M. jannaschiiencoding the proteins that are homologous to the DNA polymerase II ofP. furiosus have been located and cloned. The gene products of M. jannaschii expressed in Escherichia colihad both DNA polymerizing and 3′→5′ exonuclease activities. We propose here a novel DNA polymerase family which is entirely different from other hitherto-described DNA polymerases.

scholarly journals Roles of the Escherichia coli RecA Protein and the Global SOS Response in Effecting DNA Polymerase Selection In Vivo

2005 ◽  
Vol 187 (22) ◽  
pp. 7607-7618 ◽  
Author(s):  
Robert W. Maul ◽  
Mark D. Sutton
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Dna Polymerases ◽  
Reca Protein ◽  
Sos Response ◽  
Mutant Form ◽  
Elevated Expression ◽  
Dna Polymerase Iv ◽  
Dna Polymerase Ii

ABSTRACT The Escherichia coli β sliding clamp protein is proposed to play an important role in effecting switches between different DNA polymerases during replication, repair, and translesion DNA synthesis. We recently described how strains bearing the dnaN159 allele, which encodes a mutant form of the β clamp (β159), display a UV-sensitive phenotype that is suppressed by inactivation of DNA polymerase IV (M. D. Sutton, J. Bacteriol. 186:6738-6748, 2004). As part of an ongoing effort to understand mechanisms of DNA polymerase management in E. coli, we have further characterized effects of the dnaN159 allele on polymerase usage. Three of the five E.coli DNA polymerases (II, IV, and V) are regulated as part of the global SOS response. Our results indicate that elevated expression of the dinB-encoded polymerase IV is sufficient to result in conditional lethality of the dnaN159 strain. In contrast, chronically activated RecA protein, expressed from the recA730 allele, is lethal to the dnaN159 strain, and this lethality is suppressed by mutations that either mitigate RecA730 activity (i.e., ΔrecR), or impair the activities of DNA polymerase II or DNA polymerase V (i.e., ΔpolB or ΔumuDC). Thus, we have identified distinct genetic requirements whereby each of the three different SOS-regulated DNA polymerases are able to confer lethality upon the dnaN159 strain, suggesting the presence of multiple mechanisms by which the actions of the cell's different DNA polymerases are managed in vivo.

scholarly journals Antimutator mutations in the alpha subunit of Escherichia coli DNA polymerase III: identification of the responsible mutations and alignment with other DNA polymerases.

Genetics ◽  
1993 ◽  
Vol 134 (4) ◽  
pp. 1039-1044 ◽  
Author(s):  
I J Fijalkowska ◽  
R M Schaaper
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Dna Polymerase ◽  
Dna Polymerases ◽  
Alpha Subunit ◽  
Sequence Motifs ◽  
Dna Polymerase Iii ◽  
Conserved Sequence ◽  
Polymerase Iii ◽  
Dna Replication Errors

Abstract The dnaE gene of Escherichia coli encodes the DNA polymerase (alpha subunit) of the main replicative enzyme, DNA polymerase III holoenzyme. We have previously identified this gene as the site of a series of seven antimutator mutations that specifically decrease the level of DNA replication errors. Here we report the nucleotide sequence changes in each of the different antimutator dnaE alleles. For each a single, but different, amino acid substitution was found among the 1,160 amino acids of the protein. The observed substitutions are generally nonconservative. All affected residues are located in the central one-third of the protein. Some insight into the function of the regions of polymerase III containing the affected residues was obtained by amino acid alignment with other DNA polymerases. We followed the principles developed in 1990 by M. Delarue et al. who have identified in DNA polymerases from a large number of prokaryotic and eukaryotic sources three highly conserved sequence motifs, which are suggested to contain components of the polymerase active site. We succeeded in finding these three conserved motifs in polymerase III as well. However, none of the amino acid substitutions responsible for the antimutator phenotype occurred at these sites. This and other observations suggest that the effect of these mutations may be exerted indirectly through effects on polymerase conformation and/or DNA/polymerase interactions.

scholarly journals DNA polymerase II as a fidelity factor in chromosomal DNA synthesis in Escherichia coli

2005 ◽  
Vol 58 (1) ◽  
pp. 61-70 ◽  
Author(s):  
Magdalena Banach-Orlowska ◽  
Iwona J. Fijalkowska ◽  
Roel M. Schaaper ◽  
Piotr Jonczyk
Keyword(s):  
Escherichia Coli ◽  
Dna Synthesis ◽  
Dna Polymerase ◽  
Chromosomal Dna ◽  
Dna Polymerase Ii

scholarly journals The Escherichia coli polB gene, which encodes DNA polymerase II, is regulated by the SOS system.

1990 ◽  
Vol 172 (11) ◽  
pp. 6268-6273 ◽  
Author(s):  
H Iwasaki ◽  
A Nakata ◽  
G C Walker ◽  
H Shinagawa
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Sos System ◽  
Dna Polymerase Ii

Crystallization of DNA Polymerase II from Escherichia coli

1994 ◽  
Vol 238 (1) ◽  
pp. 120-122 ◽  
Author(s):  
Wayne F. Anderson ◽  
D.Bryan Prince ◽  
Hong Yu ◽  
Kevin McEntee ◽  
Myron F. Goodman
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Dna Polymerase Ii
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