Cloning, sequence analysis and expression in E. coli of the DNA polymerase I gene from Chloroflexus aurantiacus, a green

1998 ◽  
Vol 14 (3) ◽  
pp. 75-83 ◽  
Author(s):  
Marianne Tvermyr ◽  
Bjørn E Kristiansen ◽  
Tom Kristensen
Biochemistry ◽  
1984 ◽  
Vol 23 (9) ◽  
pp. 2073-2078 ◽  
Author(s):  
Anup K. Hazra ◽  
Sevilla Detera-Wadleigh ◽  
Samuel H. Wilson

Genetics ◽  
1990 ◽  
Vol 124 (2) ◽  
pp. 213-220 ◽  
Author(s):  
L J Reha-Krantz

Abstract Intragenic complementation was detected within the bacteriophage T4 DNA polymerase gene. Complementation was observed between specific amino (N)-terminal, temperature-sensitive (ts) mutator mutants and more carboxy (C)-terminal mutants lacking DNA polymerase polymerizing functions. Protein sequences surrounding N-terminal mutation sites are similar to sequences found in Escherichia coli ribonuclease H (RNase H) and in the 5'----3' exonuclease domain of E. coli DNA polymerase I. These observations suggest that T4 DNA polymerase, like E. coli DNA polymerase I, contains a discrete N-terminal domain.


1998 ◽  
Vol 278 (1) ◽  
pp. 147-165 ◽  
Author(s):  
Mekbib Astatke ◽  
Nigel D.F Grindley ◽  
Catherine M Joyce

1977 ◽  
Vol 78 (1) ◽  
pp. 170-176 ◽  
Author(s):  
Vito D'Aurora ◽  
Andrew M. Stern ◽  
David S. Sigman

1978 ◽  
Vol 32 (1) ◽  
pp. 25-35 ◽  
Author(s):  
D. J. Tweats ◽  
J. T. Smith

SUMMARYInitial experiments demonstrated that the plasmid R6K cannot be transferred to or maintained readily in theE. coliDNA polymerase I deficient strain JG138polA1. Results withE. coliMM386polA12(R6K), which has a temperature sensitive polymerase I enzyme, showed cell division becomes abnormal when the polymerase I enzyme of the host bacteria is inactivated at the restrictive temperature. Under conditions of polymerase I deficiency, R6K replication, as measured by monitoring R-factor-mediated β-lactamase activity, also becomes abnormal with the loss of multiple R6K copies per cell and the apparent maintenance of a single R-factor copy per cell.


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