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3
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-
0025280401
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Structural Studies of Protein-Nucleic Acid Interaction: The Sources of Sequence-Specific Binding
-
(1990)
Q Rev Biophys
, vol.23
, pp. 205-280
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-
Steitz1
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5
-
-
0025187081
-
Refinement of EcoRI Endonuclease Crystal Structure: A Revised Chain Tracing
-
The authors present revised chain tracing of the EcoRI endonuclease protein based on new isomorphous derivative data. The central kink, four-barreled helix motif and overall protein topology previously reported are unchanged, and new features include the extended-chain motif, β-bridge and the placement of Glu111.
-
(1990)
Science
, vol.249
, pp. 1307-1309
-
-
Kim1
Grable2
Love3
Greene4
Rosenberg5
-
8
-
-
0022910040
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The Effects of Base Analogue Substitutions on the Cleavage by the EcoRI Restriction Endonuclease of Octadeoxyribonucleotides Containing Modified EcoRI Recognition Sequences
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(1986)
J Biol Chem
, vol.261
, pp. 7270-7278
-
-
Brennan1
Van Cleve2
Gumport3
-
10
-
-
0025371752
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Substrate Recognition by the EcoRI Endonuclease
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This paper reports the isolation and characterization of the effects of 50 out of 60 possible mutations at the Glu144, Arg145 and Arg200 loci. Some of the mutants retain partial cleavage activity directed towards the canonical EcoRI site, leading the authors to the conclusion that the pyrimidines are contacted by additional interactions with the protein involving other amino acid residues.
-
(1990)
Proteins
, vol.7
, pp. 185-197
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-
Heitman1
Model2
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11
-
-
0024379261
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Glu-111 is Required for Activation of the DNA Cleavage Center of EcoRI Endonuclease
-
(1989)
J Biol Chem
, vol.264
, pp. 11807-11815
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-
King1
Benkovic2
Modrich3
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12
-
-
0024359479
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The Negative Charge of Glu-111 is Required to Activate the Cleavage Center of EcoRI Endonuclease
-
(1989)
J Biol Chem
, vol.264
, pp. 11816-11821
-
-
Wright1
King2
Modrich3
-
16
-
-
0025203657
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The Energetic Basis of Sequence Specificity in the Interaction of EcoRI Endonuclease with DNA
-
An exhaustive report on the kinetic and thermodynamic parameters of EcoRI endonuclease binding to, and nicking at, sites containing base analogs and substitutions. Ethylation-interference data demonstrate the existence of the canonical, isosteric and adaptive binding modes.
-
(1990)
Science
, vol.250
, pp. 776-778
-
-
Lesser1
Kurpiewski2
Jen-Jacobson3
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18
-
-
84912861917
-
-
A functional analysis of the effects of these amino acid substitutions. The ED144 mutation changed the mechanistic pathway of the enzyme from one in which double-strand cleavage is the primary result of a single binding event to one in which the enzyme rapidly dissociates after nicking the DNA.
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-
-
-
21
-
-
0025367454
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Accuracy of the EcoRI Endonuclease: Binding and Cleavage Studies with Oligodeoxynucleotide Substrates Containing Degenerate Recognition Sequences
-
∗) and base-pair mismatches within the EcoRI recognition sequence.
-
(1990)
Biochemistry
, vol.29
, pp. 4682-4691
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-
Thielking1
Alves2
Fleiss3
Maass4
Pingoud5
-
23
-
-
0024322164
-
Discrimination Between DNA Sequences by the EcoRV Restriction Endonuclease
-
2+ and nicks the DNA in a single binding event. The nicks may be repaired by DNA ligase, which inhibits the nicking in vitro.
-
(1989)
Biochemistry
, vol.28
, pp. 6198-6207
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-
Taylor1
Halford2
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25
-
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0025171673
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Mutants of the EcoRI Endonuclease with Promiscuous Substrate Specificity implicate Residues Involved in Substrate Recognition
-
(1990)
EMBO J
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Heitman1
Model2
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26
-
-
84912896058
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∗ sites in physiological buffers.
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