Structure and mechanism of DNA polymerases

被引：179

作者：

Rothwell, PJ ^{[1
]}

Waksman, G ^{[1
]}

机构：

[1] Univ London & Birkbeck Coll, Inst Struct Mol Biol, London WC1E 7HX, England

来源：

FIBROUS PROTEINS: MUSCLE AND MOLECULAR MOTORS | 2005年 / 71卷

基金：

英国惠康基金;

关键词：

D O I：

10.1016/S0065-3233(04)71011-6

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：

DNA polymerases are molecular motors directing the synthesis of DNA from nucleotides. All polymerases have a common architectural framework consisting of three canonical subdomains termed the fingers, palm, and thumb subdomains. Kinetically, they cycle through various states corresponding to conformational transitions, which may or may not generate force. In this review, we present and discuss the kinetic, structural, and single-molecule works that have contributed to our understanding of DNA polymerase function.

引用

页码：401 / +

页数：44

共 154 条

[1] EXPRESSION OF HUMAN DNA POLYMERASE-BETA IN ESCHERICHIA-COLI AND CHARACTERIZATION OF THE RECOMBINANT ENZYME [J].

ABBOTTS, J ;

SENGUPTA, DN ;

ZMUDZKA, B ;

WIDEN, SG ;

NOTARIO, V ;

WILSON, SH .

BIOCHEMISTRY, 1988, 27 (03) :901-909

[2] DNA polymerase beta: Structure-fidelity relationship from pre-steady-state kinetic analyses of all possible correct and incorrect base pairs for wild type and R283A mutant [J].

Ahn, J ;

Werneburg, BG ;

Tsai, MD .

BIOCHEMISTRY, 1997, 36 (05) :1100-1107

[3] Dependence of DNA polymerase replication rate on external forces: A model based on molecular dynamics simulations [J].

Andricioaei, I ;

Goel, A ;

Herschbach, D ;

Karplus, M .

BIOPHYSICAL JOURNAL, 2004, 87 (03) :1478-1497

[4]

[Anonymous], RETHINKING MARXISM

[5] 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

[6] IDENTIFICATION AND AMINO-ACID-SEQUENCE OF THE DEOXYNUCLEOSIDE TRIPHOSPHATE BINDING-SITE IN ESCHERICHIA-COLI DNA-POLYMERASE-I [J].

BASU, A ;

MODAK, MJ .

BIOCHEMISTRY, 1987, 26 (06) :1704-1709

[7] 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

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

BEESE, LS ;

DERBYSHIRE, V ;

STEITZ, TA .

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

[9] DNA structure and aspartate 276 influence nucleotide binding to human DNA polymerase β -: Implication for the identity of the rate-limiting conformational change [J].

Berg, BJV ;

Beard, WA ;

Wilson, SH .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (05) :3408-3416

[10] A superfamily of conserved domains in DNA damage responsive cell cycle checkpoint proteins [J].

Bork, P ;

Hofmann, K ;

Bucher, P ;

Neuwald, AF ;

Altschul, SF ;

Koonin, EV .

FASEB JOURNAL, 1997, 11 (01) :68-76

← 1 2 3 4 5 6 7 8 9 10 →