scholarly journals The origin of replication, oriC, and the dnaA protein are dispensable in stable DNA replication (sdrA) mutants of Escherichia coli K-12.

1983 ◽  
Vol 2 (3) ◽  
pp. 463-468 ◽  
Author(s):  
T. Kogoma ◽  
K. von Meyenburg
Keyword(s):  
Escherichia Coli ◽  
Dna Replication ◽  
Origin Of Replication ◽  
Dnaa Protein ◽  
Stable Dna Replication ◽  
K 12

scholarly journals Mode of initiation of constitutive stable DNA replication in RNase H-defective mutants of Escherichia coli K-12.

1987 ◽  
Vol 169 (6) ◽  
pp. 2650-2658 ◽  
Author(s):  
K von Meyenburg ◽  
E Boye ◽  
K Skarstad ◽  
L Koppes ◽  
T Kogoma
Keyword(s):  
Escherichia Coli ◽  
Dna Replication ◽  
Rnase H ◽  
Stable Dna Replication ◽  
K 12

scholarly journals RecA protein acts at the initiation of stable DNA replication in rnh mutants of Escherichia coli K-12.

1985 ◽  
Vol 163 (2) ◽  
pp. 439-444 ◽  
Author(s):  
T Kogoma ◽  
K Skarstad ◽  
E Boye ◽  
K von Meyenburg ◽  
H B Steen
Keyword(s):  
Escherichia Coli ◽  
Dna Replication ◽  
Reca Protein ◽  
Stable Dna Replication ◽  
K 12

scholarly journals Differential Suppression of priA2::kan Phenotypes in Escherichia coli K-12 by Mutations in priA, lexA, and dnaC

Genetics ◽  
1996 ◽  
Vol 143 (1) ◽  
pp. 5-13 ◽  
Author(s):  
Steven J Sandler ◽  
Hardeep S Samra ◽  
Alvin J Clark
Keyword(s):  
Escherichia Coli ◽  
Dna Replication ◽  
Mutant Allele ◽  
Wild Type ◽  
Suppressor Mutations ◽  
Dnab Helicase ◽  
K 12 ◽  
Extragenic Suppressors ◽  
Assembly Activity

Abstract First identified as an essential component of the ϕX174 in vitro DNA replication system, PriA has ATPase, helicase, translocase, and primosome-assembly activities. priA1::kan strains of Escherichia coli are sensitive to UV irradiation, deficient in homologous recombination following transduction, and filamentous. priA2::kan strains have eightfold higher levels of uninduced SOS expression than wild type. We show that (1) priA1::kan strains have eightfold higher levels of uninduced SOS expression, (2) priA2::kan strains are UVS and Rec−, (3) lexA3 suppresses the high basal levels of SOS expression of a priA2::kan strain, and (4) plasmid-encoded priA300 (K230R), a mutant allele retaining only the primosome-assembly activity of priA+, restores both UVR and Rec+ phenotypes to a priA2::kan strain. Finally, we have isolated 17 independent UVR Rec+ revertants of priA2::kan strains that carry extragenic suppressors. All 17 map in the C-terminal half of the dnaC gene. DnaC loads the DnaB helicase onto DNA as a prelude for primosome assembly and DNA replication. We conclude that priA's primosome-assembly activity is essential for DNA repair and recombination and that the dnaC suppressor mutations allow these processes to occur in the absence of priA.

scholarly journals dnaC mutations suppress defects in DNA replication- and recombination-associated functions in priB and priC double mutants in Escherichia coli K-12

1999 ◽  
Vol 34 (1) ◽  
pp. 91-101 ◽  
Author(s):  
Steven J. Sandler ◽  
Kenneth J. Marians ◽  
Kenton H. Zavitz ◽  
Jaime Coutu ◽  
Michelle A. Parent ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Replication ◽  
Associated Functions ◽  
K 12
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