Plant DNA polymerase λ, a DNA repair enzyme that functions in plant meristematic and meiotic tissues

Uchiyama, Yosuke; Kimura, Seisuke; Yamamoto, Taichi; Ishibashi, Toyotaka; Sakaguchi, Kengo

doi:10.1111/j.1432-1033.2004.04214.x

Cited by 97 publications

(90 citation statements)

References 33 publications

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“…OsEXO1 interacts with other rice DNA repair proteins: DNA polymerase λ (OsPolλ), replication protein A 70kDa subunit b (OsRPA70b), and replication protein A 32 kDa subunit (OsRPA32). These four DNA repair genes (OsEXO1, OsPolλ, OsRPA70b, and OsRPA32) are highly expressed in meristems where DNA replication is active and not in non-proliferating tissues such as mature leaves, implying their collaboration in DNA repair and replication 15,31,55 .…”

Section: Exo1/class IIImentioning

confidence: 99%

The RAD2 Family of Nucleases in Higher Plants

Furukawa¹,

Shimada²

2009

JARQ

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The RAD2 family of nucleases is a group of essential nucleases involved in 3R mechanisms (DNA replication, DNA repair and DNA recombination). The RAD2 family consists of three classes (XPG/ class I, FEN-1/class II and EXO1/class III). Recent advances in plant genome projects have revealed that in addition to plant counterparts belonging to each class of the RAD2 family higher plants have a fourth set of RAD2 family members that constitute a new class in the RAD2 family (SEND-1/class IV). DNA damage generated by endogenous or exogenous factors cause mutations that threaten the survival of plants if they are misrepaired or not repaired, which results in low crop yields. Understanding the functions of plant RAD2 family members in DNA repair is important for agricultural technology enabling an enhancement of resistance to genotoxic stresses caused by DNA damages. In this review, recent advances in our understanding of plant RAD2 family members are discussed.

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Section: Exo1/class IIImentioning

confidence: 99%

The RAD2 Family of Nucleases in Higher Plants

Furukawa¹,

Shimada²

2009

JARQ

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“…The homologue of DNA polymerase λ has recently been reported from rice 13 and Arabidopsis. 7 Genome database analyses involving rice (Oryza sativa cv.…”

Section: Structure-function Characteristics Of X-family Dna Polymerasementioning

confidence: 99%

“…Furthermore, considerable induction of Pol λ transcript in UV and MMS treated rice cells with the presence of dRP-lyase activity implicated the function of this enzyme in BER pathway in plant genome. 13 However, information are still limited regarding the structure-function characteristics of family-X DNA polymerase and other associated proteins in higher plants in relation to their functions in DNA replication and repair signaling cascade.…”

Section: Structure-function Characteristics Of X-family Dna Polymerasementioning

confidence: 99%

An insight into the biological functions of family X-DNA polymerase in DNA replication and repair of plant genome

Roy

Singh

Choudhury

et al. 2009

Plant Signaling & Behavior

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Recently we have reported the characterization of a novel single subunit 62-kDa polypeptide with ddNTP-sensitive DNA polymerase activity from the developing seeds of mungbean (Vigna radiata). The protein showed higher expression and activity level during nuclear endoreduplication stages of mungbean seeds and similarity with mammalian DNA polymerase b in many physicochemical properties. 1 The enzyme was found to specifically interact with PCNA (proliferating cell nuclear antigen), 2 and expressed in both meristematic and meiotic tissues. Functional assays have demonstrated binding of the enzyme to normal and mismatched DNA substrates and with fidelity DNA synthesis in moderately processive mode, suggesting probable involvement of the enzyme in both replication and recombination. 3 Here we have discussed the position of mungbean DNA polymerase as a homologue of DNA Pol λ, one of the newly identified member of family-X DNA polymerase in plants and illustrated the functional relevance of this enzyme in maintaining the coordination between DNA replication and repair in plant genome. Maintaining the Genome IntegrityAll living organisms are facing with the continuous challenge of maintaining the integrity of the genome to ensure faithful replication of genetic material. Thus, for replicating the genome accurately over generations, removal of damaged nucleotides and replacement with undamaged nucleotides via DNA synthesis is crucial to eliminate the chance of permanent genetic alterations. Replication and repair DNA synthesis in cells is conducted by DNA polymerases that are remarkable both in number and in functional diversity. 4 All known DNA polymerases are classified into four families such as family A (Pols γ, υ and θ), family B (Pols α, δ, ε and ζ) family Y (Pols η, ι, κ and Rev1) and family X (Pols b, λ, μ, σ1/2 and TdT, terminal deoxynucleotidyltransferase) based on their primary sequence homology. 5 In general, most enzymes belonging to families A and B are high fidelity enzymes mainly involved in faithful replication of the genome and repairing of replication error. DNA polymerases in Y-family are relatively less accurate and involved in translesion DNA synthesis, allowing replicating past stalled replication forks. On the other hand, the family-X DNA polymerases are exclusively known for their function in DNA damage repair and recombination. Structure-Function Characteristics of X-Family DNA PolymeraseMammalian family-X DNA polymerases are small, single subunit protein, relatively inaccurate enzymes and primarily involved in short gap-filling DNA synthesis of one to a few nucleotides during DNA repair processes including base excision repair (BER) and repair of double strand breaks (DSBs). With the exception of DNA Pol σ, family X polymerases are composed of a nuclear localization signal [NLS], an amino-terminal BRCT domain (similar to the BRCA1 C-terminal domain), a proline rich domain, which function as a suppressive domain for DNA Abbreviations: Pol, polymerase; BRCT, breast cancer associated C-terminus; T...

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“…Both polymerases belong to the X superfamily of DNA polymerases and several amino acid residues are conserved between POL and  (Garcia-Diaz et al, 2000;Uchiyama et al, 2004). In addition, POL has been demonstrated in rice to possess intrinsic 3'dRP activity and its expression is mainly found in meristematic and proliferating tissues (Uchiyama et al, 2004). An important role in the recognition and repair of SSB and activation of BER involves poly(ADP-ribose) polymerases (PARP).…”

Section: Fig 3 Schematic Model For Base Excision Repair (Ber)mentioning

confidence: 99%