Structure and mechanism of helicases and nucleic acid translocases

被引:968
作者
Singleton, Martin R. [1 ]
Dillingham, Mark S.
Wigley, Dale B.
机构
[1] London Res Inst, Macromol Struct & Funct Lab, London WC2A 3PX, England
[2] Univ Bristol, Sch Med Sci, Dept Biochem, DNA Prot Interact Unit, Bristol BS8 1TD, Avon, England
[3] London Res Inst, Mol Enzymol Lab, S Mimms EN6 3LD, Herts, England
关键词
ATPase; DNTA repair; DNA replication translocase; HEPATITIS-C VIRUS; SINGLE-STRANDED-DNA; REPLICATIVE HEXAMERIC HELICASE; BACTERIOPHAGE-T4 DDA HELICASE; CHROMATIN-REMODELING ENZYME; TERMINATION FACTOR-RHO; COLI REP HELICASE; BOX RNA HELICASE; CRYSTAL-STRUCTURE; PCRA HELICASE;
D O I
10.1146/annurev.biochem.76.052305.115300
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
Helicases and translocases are a ubiquitous, highly diverse group of proteins that perform an extraordinary variety of functions in cells. Consequently, this review sets out to define a nomenclature for these enzymes based on current knowledge of sequence, structure, and mechanism. Using previous definitions of helicase families as a basis, we delineate six superfamilies of enzymes, with examples of crystal structures where available, and discuss these structures in the context of biochemical data to outline our present understanding of helicase and translocase activity. As a result, each superfamily is subdivided, where appropriate, on the basis of mechanistic understanding, which we hope will provide a framework for classification of new superfamily members as they are discovered and characterized.
引用
收藏
页码:23 / 50
页数:28
相关论文
共 121 条
[51]   The DExH protein NPH-II is a processive and directional motor for unwinding RNA [J].
Jankowsky, E ;
Gross, CH ;
Shuman, S ;
Pyle, AM .
NATURE, 2000, 403 (6768) :447-451
[52]   Active disruption of an RNA-protein interaction by a DExH/D RNA helicase [J].
Jankowsky, E ;
Gross, CH ;
Shuman, S ;
Pyle, AM .
SCIENCE, 2001, 291 (5501) :121-125
[53]   Rad54p is a chromatin remodeling enzyme required for heteroduplex DNA joint formation with chromatin [J].
Jaskelioff, M ;
Van Komen, S ;
Krebs, JE ;
Sung, P ;
Peterson, CL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (11) :9212-9218
[54]   The 3′-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase [J].
Kaplan, DL .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 301 (02) :285-299
[55]   Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes [J].
Kaplan, DL ;
O'Donnell, M .
MOLECULAR CELL, 2004, 15 (03) :453-465
[56]   Backbone tracking by the SF2 helicase NPH-II [J].
Kawaoka, J ;
Jankowsky, E ;
Pyle, AM .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2004, 11 (06) :526-530
[57]   T7 DNA helicase: A molecular motor that processively and unidirectionally translocates along single-stranded DNA [J].
Kim, DE ;
Narayan, M ;
Patel, SS .
JOURNAL OF MOLECULAR BIOLOGY, 2002, 321 (05) :807-819
[58]   Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding [J].
Kim, JL ;
Morgenstern, KA ;
Griffith, JP ;
Dwyer, MD ;
Thomson, JA ;
Murcko, MA ;
Lin, C ;
Caron, PR .
STRUCTURE, 1998, 6 (01) :89-100
[59]   Structurally conserved amino acid W501 is required for RNA helicase activity but is not essential for DNA helicase activity of hepatitis C virus NS3 protein [J].
Kim, JW ;
Seo, MY ;
Shelat, A ;
Kim, CS ;
Kwon, TW ;
Lu, HH ;
Moustakas, DT ;
Sun, J ;
Han, JH .
JOURNAL OF VIROLOGY, 2003, 77 (01) :571-582
[60]   Major domain swiveling revealed by the crystal structures of complexes of E-coli Rep helicase bound to single-stranded DNA and ADP [J].
Korolev, S ;
Hsieh, J ;
Gauss, GH ;
Lohman, TM ;
Waksman, G .
CELL, 1997, 90 (04) :635-647