Suppressor mutations (rin) that specifically suppress the recA + dependence of stable DNA replication in Escherichia coli K-12

1982 ◽  
Vol 187 (2) ◽  
pp. 225-230 ◽  
Author(s):  
Ted Albert Torrey ◽  
Tokio Kogoma
Genetics ◽  
1996 ◽  
Vol 143 (1) ◽  
pp. 5-13 ◽  
Author(s):  
Steven J Sandler ◽  
Hardeep S Samra ◽  
Alvin J Clark

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.


1987 ◽  
Vol 169 (6) ◽  
pp. 2650-2658 ◽  
Author(s):  
K von Meyenburg ◽  
E Boye ◽  
K Skarstad ◽  
L Koppes ◽  
T Kogoma

1985 ◽  
Vol 163 (2) ◽  
pp. 439-444 ◽  
Author(s):  
T Kogoma ◽  
K Skarstad ◽  
E Boye ◽  
K von Meyenburg ◽  
H B Steen

1999 ◽  
Vol 34 (1) ◽  
pp. 91-101 ◽  
Author(s):  
Steven J. Sandler ◽  
Kenneth J. Marians ◽  
Kenton H. Zavitz ◽  
Jaime Coutu ◽  
Michelle A. Parent ◽  
...  

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