The Conserved Motif in Hydrophilic Loop 2/3 and Loop 8/9 of the Lactose Permease of Escherichia coli. Analysis of Suppressor Mutations

2000 ◽  
Vol 176 (2) ◽  
pp. 159-168 ◽  
Author(s):  
S.M. Cain ◽  
E.A. Matzke ◽  
R.J. Brooker

1995 ◽  
Vol 270 (27) ◽  
pp. 16251-16257 ◽  
Author(s):  
Amy E. Jessen-Marshall ◽  
Nanette J. Paul ◽  
Robert J. Brooker


2000 ◽  
Vol 174 (1) ◽  
pp. 31-40 ◽  
Author(s):  
N.J. Pazdernik ◽  
E.A. Matzke ◽  
A.E. Jessen-Marshall ◽  
R.J. Brooker


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.





Biochemistry ◽  
1995 ◽  
Vol 34 (4) ◽  
pp. 1107-1112 ◽  
Author(s):  
Miklos Sahin-Toth ◽  
Rhonda L. Dunten ◽  
H. Ronald Kaback


1988 ◽  
Vol 263 (31) ◽  
pp. 15906-15914 ◽  
Author(s):  
M G Page ◽  
J P Rosenbusch




1990 ◽  
Vol 10 (5) ◽  
pp. 1908-1914
Author(s):  
C Martin ◽  
S Okamura ◽  
R Young

The two large subunits of RNA polymerase II, RPB1 and RPB2, contain regions of extensive homology to the two large subunits of Escherichia coli RNA polymerase. These homologous regions may represent separate protein domains with unique functions. We investigated whether suppressor genetics could provide evidence for interactions between specific segments of RPB1 and RPB2 in Saccharomyces cerevisiae. A plasmid shuffle method was used to screen thoroughly for mutations in RPB2 that suppress a temperature-sensitive mutation, rpb1-1, which is located in region H of RPB1. All six RPB2 mutations that suppress rpb1-1 were clustered in region I of RPB2. The location of these mutations and the observation that they were allele specific for suppression of rpb1-1 suggests an interaction between region H of RPB1 and region I of RPB2. A similar experiment was done to isolate and map mutations in RPB1 that suppress a temperature-sensitive mutation, rpb2-2, which occurs in region I of RPB2. These suppressor mutations were not clustered in a particular region. Thus, fine structure suppressor genetics can provide evidence for interactions between specific segments of two proteins, but the results of this type of analysis can depend on the conditional mutation to be suppressed.



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