Active Site Interactions Impact Phosphoryl Transfer during Replication of Damaged and Undamaged DNA by Escherichia coli DNA Polymerase I

Chemical Research in Toxicology ◽

10.1021/acs.chemrestox.7b00257 ◽

2017 ◽

Vol 30 (11) ◽

pp. 2033-2043

Author(s):

A. S. Prakasha Gowda ◽

Thomas E. Spratt

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Active Site ◽

Phosphoryl Transfer ◽

Dna Polymerase I ◽

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The 3′-5′ exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction.

The EMBO Journal ◽

10.1002/j.1460-2075.1991.tb07916.x ◽

1991 ◽

Vol 10 (1) ◽

pp. 17-24 ◽

Author(s):

V. Derbyshire ◽

N. D. Grindley ◽

C. M. Joyce

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Active Site ◽

Dna Polymerase I ◽

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Point mutations which drastically affect the polymerization activity of encephalomyocarditis virus RNA-dependent RNA polymerase correspond to the active site of Escherichia coli DNA polymerase I.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)50215-0 ◽

1992 ◽

Vol 267 (14) ◽

pp. 10168-10176

Author(s):

S Sankar ◽

A.G. Porter

Keyword(s):

Escherichia Coli ◽

Rna Polymerase ◽

Dna Polymerase ◽

Active Site ◽

Point Mutations ◽

Encephalomyocarditis Virus ◽

Dna Polymerase I ◽

Rna Dependent Rna Polymerase ◽

Virus Rna ◽

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Reactions at the polymerase active site that contribute to the fidelity of Escherichia coli DNA polymerase I (Klenow fragment).

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)35792-2 ◽

1992 ◽

Vol 267 (34) ◽

pp. 24485-24500 ◽

Author(s):

C.M. Joyce ◽

X.C. Sun ◽

N.D. Grindley

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Active Site ◽

Klenow Fragment ◽

Dna Polymerase I ◽

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Faculty Opinions recommendation of Targeted gene evolution in Escherichia coli using a highly error-prone DNA polymerase I.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1014299.195701 ◽

2003 ◽

Author(s):

Frances Arnold

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Gene Evolution ◽

Dna Polymerase I ◽

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Oxygen-dependent cleavage of DNA by the 1,10-phenanthroline . cuprous complex. Inhibition of Escherichia coli DNA polymerase I.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)86305-6 ◽

1979 ◽

Vol 254 (24) ◽

pp. 12269-12272

Author(s):

D.S. Sigman ◽

D.R. Graham ◽

V. D'Aurora ◽

A.M. Stern

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Dna Polymerase I ◽

Polymerase I ◽

Cuprous Complex

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Studies on the mechanism of Escherichia coli DNA polymerase I large fragment. Chain termination and modulation by polynucleotides.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)34139-5 ◽

1982 ◽

Vol 257 (16) ◽

pp. 9770-9780 ◽

Author(s):

S D Detera ◽

S H Wilson

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Chain Termination ◽

Large Fragment ◽

Dna Polymerase I ◽

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D(M6ATP) as a probe of the fidelity of base incorporation into polynucleotides by Escherichia coli DNA polymerase I.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)38194-2 ◽

1978 ◽

Vol 253 (3) ◽

pp. 935-939

Author(s):

J.D. Engel ◽

P.H. von Hippel

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Dna Polymerase I ◽

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On the processive mechanism of Escherichia coli DNA polymerase I. Delayed initiation of polymerization.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)33359-8 ◽

1976 ◽

Vol 251 (13) ◽

pp. 4090-4094 ◽

Author(s):

R A Bambara ◽

D Uyemura ◽

I R Lehman

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Dna Polymerase I ◽

Delayed Initiation ◽

Polymerase I ◽

Initiation Of Polymerization

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Biochemical characterization of mutant forms of DNA polymerase I from Escherichia coli. I. The polA12 mutation.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)33357-4 ◽

1976 ◽

Vol 251 (13) ◽

pp. 4078-4084 ◽

Author(s):

D Uyemura ◽

I R Lehman

Keyword(s):

Escherichia Coli ◽

Dna Polymerase ◽

Biochemical Characterization ◽

Dna Polymerase I ◽

Polymerase I ◽

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Template primer-dependent binding of 5'-fluorosulfonyl-benzoyldeoxyadenosine by Escherichia coli DNA polymerase I. Identification of arginine 682 as the binding site and its implication in catalysis.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)39647-4 ◽

1990 ◽

Vol 265 (7) ◽

pp. 3679-3684

Author(s):

V N Pandey ◽

N A Kaushik ◽

D S Pradhan ◽

M J Modak

Keyword(s):

Escherichia Coli ◽

Binding Site ◽

Dna Polymerase ◽

Dna Polymerase I ◽

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