Phylogenetic analysis and evolutionary origins of DNA polymerase X-family members

被引:24
作者
Bienstock, Rachelle J. [1 ]
Beard, William A. [1 ]
Wilson, Samuel H. [1 ]
机构
[1] NIEHS, Struct Biol Lab, NIH, Res Triangle Pk, NC 27709 USA
基金
美国国家卫生研究院;
关键词
DNA polymerase; Evolution; Genomics; Phylogenetic; Structure-function; X-family; SITE-DIRECTED MUTAGENESIS; MULTIPLE SEQUENCE ALIGNMENT; THERMUS-THERMOPHILUS HB8; AMINO-ACID SUBSTITUTION; STATE KINETIC ANALYSES; ACTIVE-SITE; DEINOCOCCUS-RADIODURANS; SUBSTRATE-SPECIFICITY; NUCLEOTIDYL TRANSFER; EXONUCLEASE ACTIVITY;
D O I
10.1016/j.dnarep.2014.07.003
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Mammalian DNA polymerase (pol) beta is the founding member of a large group of DNA polymerases now termed the X-family. DNA polymerase beta has been kinetically, structurally, and biologically well characterized and can serve as a phylogenetic reference. Accordingly, we have performed a phylogenetic analysis to understand the relationship between pol beta and other members of the X-family of DNA polymerases. The bacterial X-family DNA polymerases, Saccharomyces cerevisiae pol IV, and four mammalian X-family polymerases appear to be directly related. These enzymes originated from an ancient common ancestor characterized in two Bacillus species. Understanding distinct functions for each of the X-family polymerases, evolving from a common bacterial ancestor is of significant interest in light of the specialized roles of these enzymes in DNA metabolism. Published by Elsevier B.V.
引用
收藏
页码:77 / 88
页数:12
相关论文
共 76 条
[51]   EXCISION OF DEOXYRIBOSE PHOSPHATE RESIDUES BY DNA-POLYMERASE-BETA DURING DNA-REPAIR [J].
MATSUMOTO, Y ;
KIM, K .
SCIENCE, 1995, 269 (5224) :699-702
[52]   Structure-function analysis of the mammalian DNA polymerase beta active site: Role of aspartic acid 256, arginine 254, and arginine 258 in nucleotidyl transfer [J].
Menge, KL ;
Hostomsky, Z ;
Nodes, BR ;
Hudson, GO ;
Rahmati, S ;
Moomaw, EW ;
Almassy, RJ ;
Hostomska, Z .
BIOCHEMISTRY, 1995, 34 (49) :15934-15942
[53]   8-OxodGTP incorporation by DNA polymerase β is modified by active-site residue Asn279 [J].
Miller, H ;
Prasad, R ;
Wilson, SH ;
Johnson, F ;
Grollman, AP .
BIOCHEMISTRY, 2000, 39 (05) :1029-1033
[54]   The X family portrait: Structural insights into biological functions of X family polymerases [J].
Moon, Andrea F. ;
Garcia-Diaz, Miguel ;
Batra, Vinod K. ;
Beard, William A. ;
Bebenek, Katarzyna ;
Kunkel, Thomas A. ;
Wilson, Samuel H. ;
Pedersen, Lars C. .
DNA REPAIR, 2007, 6 (12) :1709-1725
[55]   Structural insight into the substrate specificity of DNA Polymerase μ [J].
Moon, Andrea F. ;
Garcia-Diaz, Miguel ;
Bebenek, Katarzyna ;
Davis, Bryan J. ;
Zhong, Xuejun ;
Ramsden, Dale A. ;
Kunkel, Thomas A. ;
Pedersen, Lars C. .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2007, 14 (01) :45-53
[56]   The Structural Basis of the Kinetic Mechanism of a Gap-Filling X-Family DNA Polymerase That Binds Mg2+-dNTP Before Binding to DNA [J].
Nakane, Shuhei ;
Ishikawa, Hirohito ;
Nakagawa, Noriko ;
Kuramitsu, Seiki ;
Masui, Ryoji .
JOURNAL OF MOLECULAR BIOLOGY, 2012, 417 (03) :179-196
[57]   Characterization of DNA polymerase X from Thermus thermophilus HB8 reveals the POLXc and PHP domains are both required for 35 exonuclease activity [J].
Nakane, Shuhei ;
Nakagawa, Noriko ;
Kuramitsu, Seiki ;
Masui, Ryoji .
NUCLEIC ACIDS RESEARCH, 2009, 37 (06) :2037-2052
[58]   Characterization of an African swine fever virus 20-kDa DNA polymerase involved in DNA repair [J].
Oliveros, M ;
Yáñez, RJ ;
Salas, ML ;
Salas, J ;
Viñuela, E ;
Blanco, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (49) :30899-30910
[59]   The mutator form of polymerase β with amino acid substitution at tyrosine 265 in the hinge region displays an increase in both base substitution and frame shift errors [J].
Opresko, PL ;
Sweasy, JB ;
Eckert, KA .
BIOCHEMISTRY, 1998, 37 (08) :2111-2119
[60]   Base substitution specificity of DNA polymerase β depends on interactions in the DNA minor groove [J].
Osheroff, WP ;
Beard, WA ;
Wilson, SH ;
Kunkel, TK .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (30) :20749-20752