The mechanism of action of T7 DNA polymerase

被引：166

作者：

Doublié, S ^{[1
]}

Ellenberger, T ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1998年 / 8卷 / 06期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0959-440X(98)80089-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The recent crystal structure determination of T7 DNA polymerase complexed to a deoxynucleoside triphosphate and primer-template DNA has provided the first glimpse of a replicative DNA polymerase in a catalytic complex. The structure complements many functional and structural studies of this and other DNA polymerases, allowing a detailed evaluation of proposals for the mechanism of nucleotidyl transfer and the exploration of the basis for the high fidelity of template-directed DNA synthesis.

引用

页码：704 / 712

页数：9

共 70 条

[1] MAPPING THE TRANSITION-STATE FOR ATP HYDROLYSIS - IMPLICATIONS FOR ENZYMATIC CATALYSIS [J].

ADMIRAAL, SJ ;

HERSCHLAG, D .

CHEMISTRY & BIOLOGY, 1995, 2 (11) :729-739

[2] DEOXYNUCLEOSIDE TRIPHOSPHATE AND PYROPHOSPHATE BINDING-SITES IN THE CATALYTICALLY COMPETENT TERNARY COMPLEX FOR THE POLYMERASE REACTION CATALYZED BY DNA-POLYMERASE-I (KLENOW FRAGMENT) [J].

ASTATKE, M ;

GRINDLEY, NDF ;

JOYCE, CM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (04) :1945-1954

[3] How E-coli DNA polymerase I (Klenow fragment) distinguishes between deoxy- and dideoxynucleotides [J].

Astatke, M ;

Grindley, NDF ;

Joyce, CM .

JOURNAL OF MOLECULAR BIOLOGY, 1998, 278 (01) :147-165

[4] A single side chain prevents Escherichia coli DNA polymerase I (Klenow fragment) from incorporating ribonucleotides [J].

Astatke, M ;

Ng, KM ;

Grindley, NDF ;

Joyce, CM .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (07) :3402-3407

[5] Polymerases and the replisome: Machines within machines [J].

Baker, TA ;

Bell, SP .

CELL, 1998, 92 (03) :295-305

[6] The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on Escherichia coli DNA polymerase I [J].

Bedford, E ;

Tabor, S ;

Richardson, CC .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (02) :479-484

[7] STRUCTURAL BASIS FOR THE 3'-5' EXONUCLEASE ACTIVITY OF ESCHERICHIA-COLI DNA-POLYMERASE-I - A 2 METAL-ION MECHANISM [J].

BEESE, LS ;

STEITZ, TA .

EMBO JOURNAL, 1991, 10 (01) :25-33

[8] CRYSTAL-STRUCTURES OF THE KLENOW FRAGMENT OF DNA-POLYMERASE-I COMPLEXED WITH DEOXYNUCLEOSIDE TRIPHOSPHATE AND PYROPHOSPHATE [J].

BEESE, LS ;

FRIEDMAN, JM ;

STEITZ, TA .

BIOCHEMISTRY, 1993, 32 (51) :14095-14101

[9] STRUCTURE OF DNA-POLYMERASE-I KLENOW FRAGMENT BOUND TO DUPLEX DNA [J].

BEESE, LS ;

DERBYSHIRE, V ;

STEITZ, TA .

SCIENCE, 1993, 260 (5106) :352-355

[10] Base miscoding and strand misalignment errors by mutator klenow polymerases with amino acid substitutions at tyrosine 766 in the O helix of the fingers subdomain [J].

Bell, JB ;

Eckert, KA ;

Joyce, CM ;

Kunkel, TA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (11) :7345-7351

← 1 2 3 4 5 6 7 →