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

来源：

DNA REPAIR | 2014年 / 22卷

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

页码：77 / 88

页数：12

共 76 条

[1] 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

[2] An intrinsic 5′-deoxyribose-5-phosphate lyase activity in DNA polymerase beta from Leishmania infantum supports a role in DNA repair [J].

Alonso, A ;

Terrados, G ;

Picher, AJ ;

Giraldo, R ;

Blanco, L ;

Larraga, V .

DNA REPAIR, 2006, 5 (01) :89-101

[3] DNA polymerase β-like nucleotidyltransferase superfamily:: identification of three new families, classification and evolutionary history [J].

Aravind, L ;

Koonin, EV .

NUCLEIC ACIDS RESEARCH, 1999, 27 (07) :1609-1618

[4] Single-nucleotide base excision repair DNA polymerase activity in C. elegans in the absence of DNA polymerase β [J].

Asagoshi, Kenjiro ;

Lehmann, Wade ;

Braithwaite, Elena K. ;

Santana-Santos, Lucas ;

Prasad, Rajendra ;

Freedman, Jonathan H. ;

Van Houten, Bennett ;

Wilson, Samuel H. .

NUCLEIC ACIDS RESEARCH, 2012, 40 (02) :670-681

[5] The structure of T-aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases [J].

Bailey, Scott ;

Wing, Richard A. ;

Steitz, Thomas A. .

CELL, 2006, 126 (05) :893-904

[6] Contribution of the Reverse Rate of the Conformational Step to Polymerise β Fidelity [J].

Bakhtina, Marina ;

Roettger, Michelle P. ;

Tsai, Ming-Daw .

BIOCHEMISTRY, 2009, 48 (14) :3197-3208

[7] Editing of misaligned 3′-termini by an intrinsic 3′-5′ exonuclease activity residing in the PHP domain of a family X DNA polymerase [J].

Banos, Benito ;

Lazaro, Jose M. ;

Villar, Laurentino ;

Salas, Margarita ;

de Vega, Miguel .

NUCLEIC ACIDS RESEARCH, 2008, 36 (18) :5736-5749

[8] Intrinsic apurinic/apyrimidinic (AP) endonuclease activity enables Bacillus subtilis DNA polymerase X to recognize, incise, and further repair abasic sites [J].

Banos, Benito ;

Villar, Laurentino ;

Salas, Margarita ;

de Vega, Miguel .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (45) :19219-19224

[9] Characterization of a Bacillus subtilis 64-kDa DNA Polymerase X Potentially Involved in DNA Repair [J].

Banos, Benito ;

Lazaro, Jose M. ;

Villar, Laurentino ;

Salas, Margarita ;

de Vega, Miguel .

JOURNAL OF MOLECULAR BIOLOGY, 2008, 384 (05) :1019-1028

[10] Amino Acid Substitution in the Active Site of DNA Polymerase β Explains the Energy Barrier of the Nucleotidyl Transfer Reaction [J].

Batra, Vinod K. ;

Perera, Lalith ;

Lin, Ping ;

Shock, David D. ;

Beard, William A. ;

Pedersen, Lars C. ;

Pedersen, Lee G. ;

Wilson, Samuel H. .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2013, 135 (21) :8078-8088

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