Motors, Switches, and Contacts in the Replisome

被引:128
作者
Hamdan, Samir M. [1 ]
Richardson, Charles C. [1 ]
机构
[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA
关键词
DNA; helicase; Okazaki fragments; polymerase; primase; processivity; replication; replication fork; SINGLE-STRANDED-DNA; POLYMERASE-III HOLOENZYME; BACTERIOPHAGE-T7; DEOXYRIBONUCLEIC-ACID; ESCHERICHIA-COLI THIOREDOXIN; PROTEIN-PROTEIN INTERACTIONS; RNA PRIMER SYNTHESIS; COORDINATED LEADING-STRAND; GENE-4; HELICASE-PRIMASE; OKAZAKI FRAGMENT SYNTHESIS; REPLICATION-FORK HELICASE;
D O I
10.1146/annurev.biochem.78.072407.103248
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
Replisomes are the protein assemblies that replicate DNA. They function as molecular motors to catalyze template-mediated polymerization of nucleotides, unwinding of DNA, the synthesis of RNA primers, and the assembly of proteins on DNA. The replisome of bacteriophage T7 contains a minimum of proteins, thus facilitating its study. This review describes the molecular motors and coordination of their activities, with emphasis on the T7 replisome. Nucleotide selection, movement of the polymerase, binding of the processivity factor, unwinding of DNA, and RNA primer synthesis all require conformational changes and protein contacts. Lagging-strand synthesis is mediated via a replication loop whose formation and resolution is dictated by switches to yield Okazaki fragments of discrete size. Both strands are synthesized at identical rates, controlled by a molecular brake that halts leading-strand synthesis during primer synthesis. The helicase serves as a reservoir for polymerases that can initiate DNA synthesis at the replication fork. We comment on the differences in other systems where applicable.
引用
收藏
页码:205 / 243
页数:39
相关论文
共 238 条
[1]   A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein [J].
Ahnert, P ;
Picha, KM ;
Patel, SS .
EMBO JOURNAL, 2000, 19 (13) :3418-3427
[2]   STUDIES ON DNA-REPLICATION IN THE BACTERIOPHAGE-T4 INVITRO SYSTEM [J].
ALBERTS, BM ;
BARRY, J ;
BEDINGER, P ;
FORMOSA, T ;
JONGENEEL, CV ;
KREUZER, KN .
COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY, 1982, 47 :655-668
[3]  
ALLEN GC, 1993, J BIOL CHEM, V268, P19204
[4]   The carboxyl terminus of the bacteriophage T4 DNA polymerase contacts its sliding clamp at the subunit interface [J].
Alley, SC ;
Jones, AD ;
Soumillion, P ;
Benkovic, SJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (35) :24485-24489
[5]   Tracking sliding clamp opening and closing during bacteriophage T4 DNA polymerase holoenzyme assembly [J].
Alley, SC ;
Abel-Santos, E ;
Benkovic, SJ .
BIOCHEMISTRY, 2000, 39 (11) :3076-3090
[6]   Sliding clamp of the bacteriophage T4 polymerase has open and closed subunit interfaces in solution [J].
Alley, SC ;
Shier, VK ;
Abel-Santos, E ;
Sexton, DJ ;
Soumillion, P ;
Benkovic, SJ .
BIOCHEMISTRY, 1999, 38 (24) :7696-7709
[7]   Building a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerise holoenzyme [J].
Alley, SC ;
Trakselis, MA ;
Mayer, MU ;
Ishmael, FT ;
Jones, AD ;
Benkovic, SJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (42) :39340-39349
[8]   The highly processive DNA polymerase of bacteriophage T5 - Role of the unique N and C termini [J].
Andraos, N ;
Tabor, S ;
Richardson, CC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (48) :50609-50618
[9]   Toprim - a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins [J].
Aravind, L ;
Leipe, DD ;
Koonin, EV .
NUCLEIC ACIDS RESEARCH, 1998, 26 (18) :4205-4213
[10]   A model for Escherichia coli DNA polymerase III holoenzyme assembly at primer/template ends -: DNA triggers a change in binding specificity of the γ complex clamp loader [J].
Ason, B ;
Bertram, JG ;
Hingorani, MM ;
Beechem, JM ;
O'Donnell, M ;
Goodman, MF ;
Bloom, LB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (04) :3006-3015