Plant DNA polymerases α and δ mediate replication of geminiviruses

AbstractGeminiviruses are causal agents of devastating diseases in crops. Geminiviruses have circular single-stranded (ss) DNA genomes that are replicated in the nucleus of the infected plant cell through double-stranded (ds) DNA intermediates by the plant DNA replication machinery. Which host DNA polymerase mediates geminiviral multiplication, however, has so far remained elusive. Here, we show that subunits of the nuclear replicative DNA polymerases α and δ physically interact with the geminivirus-encoded replication enhancer protein, C3, and that these polymerases are required for viral replication. Our results suggest that, while DNA polymerase α is essential to generate the viral dsDNA intermediate, DNA polymerase δ mediates the synthesis of new copies of the geminiviral ssDNA genome, and that the virus-encoded C3 may act selectively, recruiting DNA polymerase δ over ε to favour productive replication.

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Plant DNA polymerases alpha and delta mediate replication of geminiviruses

10.1101/2020.07.20.212167 ◽

2020 ◽

Cited By ~ 1

Author(s):

Mengshi Wu ◽

Hua Wei ◽

Huang Tan ◽

Shaojun Pan ◽

Qi Liu ◽

...

Keyword(s):

Dna Replication ◽

Viral Replication ◽

Dna Polymerase ◽

Plant Cell ◽

Dna Polymerases ◽

Infected Plant ◽

Replication Machinery ◽

Dna Polymerase Δ ◽

Dna Polymerase Α ◽

Productive Replication

ABSTRACTGeminiviruses are causal agents of devastating diseases in crops. Geminiviruses have circular single-stranded (ss)DNA genomes that are replicated in the nucleus of the infected plant cell through double-stranded (ds)DNA intermediates by the plant’s DNA replication machinery; which host DNA polymerase mediates geminiviral multiplication, however, has so far remained elusive. Here, we show that subunits of the nuclear replicative DNA polymerases α and δ physically interact with the geminivirus-encoded replication enhancer protein, C3, and are required for viral replication. Our results suggest that while DNA polymerase α is essential to generate the viral dsDNA intermediate, DNA polymerase δ mediates the synthesis of new copies of the geminiviral ssDNA genome, and that the virus-encoded C3 acts selectively recruiting DNA polymerase δ over ε to favour a productive replication.

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Role of Translesion Synthesis DNA Polymerases in DNA Replication in the Presence of a Weak DNA Polymerase δ in Saccharomyces cerevisiae

G3 Genes|Genome|Genetics ◽

10.1534/g3.118.200213 ◽

2018 ◽

Vol 8 (2) ◽

pp. 754-754

Author(s):

Likui Zhang ◽

Yanchao Huang ◽

Xinyuan Zhu ◽

Yuxiao Wang ◽

Haoqiang Shi ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Dna Replication ◽

Dna Polymerase ◽

Dna Polymerases ◽

Translesion Synthesis ◽

Dna Polymerase Δ

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The TREX2 3′→ 5′ Exonuclease Physically Interacts with DNA Polymerase δ and Increases Its Accuracy

The Scientific World JOURNAL ◽

10.1100/tsw.2002.99 ◽

2002 ◽

Vol 2 ◽

pp. 275-281 ◽

Cited By ~ 15

Author(s):

Igor V. Shevelev ◽

Kristijan Ramadan ◽

Ulrich Hubscher

Keyword(s):

Dna Replication ◽

Dna Polymerase ◽

Error Rates ◽

High Fidelity ◽

Replication Machinery ◽

Dna Polymerase Δ ◽

Pol I ◽

Calf Thymus ◽

Mutation Assay ◽

Forward Mutation

Proofreading function by the 3′→ 5′ exonuclease of DNA polymerase δ (pol δ) is consistent with the observation that deficiency of the associated exonuclease can lead to a strong mutation phenotype, high error rates during DNA replication, and ultimately cancer. We have isolated pol δdfrom isotonic (pol δi) and detergent (pol δd) calf thymus extracts. Pol δdhad a 20-fold higher ratio of exonuclease to DNA polymerase than pol δi. This was due to the physical association of the TREX2 exonuclease to pol δd, which was missing from pol δi. Pol δdwas fivefold more accurate than pol δiunder error-prone conditions (1 μM dGTP and 20 dATP, dCTP, and dTTP) in a M13mp2 DNA forward mutation assay, and fourfold more accurate in an M13mp2T90 reversion assay. Under error-free conditions (20 μM each of the four dNTPs), however, both polymerases showed equal fidelity. Our data suggested that autonomous 3′→ 5′ exonucleases, such as TREX2, through its association with pol I can guarantee high fidelity under difficult conditions in the cell (e.g., imbalance of dNTPs) and can add to the accuracy of the DNA replication machinery, thus preventing mutagenesis.

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Role of Translesion Synthesis DNA Polymerases in DNA Replication in the Presence of a Weak DNA Polymerase δ in Saccharomyces cerevisiae

G3 Genes|Genome|Genetics ◽

10.1534/g3.117.300097 ◽

2017 ◽

Vol 8 (2) ◽

pp. 754-754

Author(s):

Likui Zhang ◽

Yanchao Huang ◽

Xinyuan Zhu ◽

Yuxiao Wang ◽

Haoqiang Shi ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Dna Replication ◽

Dna Polymerase ◽

Dna Polymerases ◽

Translesion Synthesis ◽

Dna Polymerase Δ

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The N-Terminal Noncatalytic Region of Xenopus RecQ4 Is Required for Chromatin Binding of DNA Polymerase α in the Initiation of DNA Replication

Molecular and Cellular Biology ◽

10.1128/mcb.02267-05 ◽

2006 ◽

Vol 26 (13) ◽

pp. 4843-4852 ◽

Cited By ~ 110

Author(s):

Kumiko Matsuno ◽

Maya Kumano ◽

Yumiko Kubota ◽

Yoshitami Hashimoto ◽

Haruhiko Takisawa

Keyword(s):

Dna Replication ◽

Dna Polymerase ◽

Sequence Similarity ◽

Dna Polymerases ◽

Helicase Domain ◽

Chromatin Binding ◽

Replication Machinery ◽

Dna Polymerase Α ◽

Initiation Of Dna Replication ◽

Replication Activity

ABSTRACT Recruitment of DNA polymerases onto replication origins is a crucial step in the assembly of eukaryotic replication machinery. A previous study in budding yeast suggests that Dpb11 controls the recruitment of DNA polymerases α and ε onto the origins. Sld2 is an essential replication protein that interacts with Dpb11, but no metazoan homolog has yet been identified. We isolated Xenopus RecQ4 as a candidate Sld2 homolog. RecQ4 is a member of the metazoan RecQ helicase family, and its N-terminal region shows sequence similarity with Sld2. In Xenopus egg extracts, RecQ4 is essential for the initiation of DNA replication, in particular for chromatin binding of DNA polymerase α. An N-terminal fragment of RecQ4 devoid of the helicase domain could rescue the replication activity of RecQ4-depleted extracts, and antibody against the fragment inhibited DNA replication and chromatin binding of the polymerase. Further, N-terminal fragments of RecQ4 physically interacted with Cut5, a Xenopus homolog of Dpb11, and their ability to bind to Cut5 closely correlated with their ability to rescue the replication activity of the depleted extracts. Our data suggest that RecQ4 performs an essential role in the assembly of replication machinery through interaction with Cut5 in vertebrates.

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DNA Replication Machinery: Functional Characterization of a Complex Containing DNA Polymerase α, DNA Polymerase δ, and Replication Factor C Suggests an Asymmetric DNA Polymerase Dimer†

Biochemistry ◽

10.1021/bi952455k ◽

1996 ◽

Vol 35 (18) ◽

pp. 5764-5777 ◽

Cited By ~ 31

Author(s):

Giovanni Maga ◽

Ulrich Hübscher

Keyword(s):

Dna Replication ◽

Dna Polymerase ◽

Functional Characterization ◽

Replication Factor C ◽

Replication Machinery ◽

Replication Factor ◽

Dna Polymerase Δ ◽

Dna Polymerase Α ◽

Factor C

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PrimPol (Primase/Polymerase), replicating enzyme – A mini review

Pak-Euro Journal of Medical and Life Sciences ◽

10.31580/pjmls.v2i4.956 ◽

2020 ◽

Vol 2 (4) ◽

pp. 89-92

Author(s):

Muhammad Amir ◽

Sabeera Afzal ◽

Alia Ishaq

Keyword(s):

Dna Replication ◽

Dna Polymerase ◽

Genetic Information ◽

Nuclear Dna ◽

De Novo ◽

Dna Polymerases ◽

Test Site ◽

Mitochondrial Dna Replication ◽

Dna Template ◽

Preliminary Phase

Polymerases were revealed first in 1970s. Most important to the modest perception the enzyme responsible for nuclear DNA replication that was pol , for DNA repair pol and for mitochondrial DNA replication pol DNA construction and renovation done by DNA polymerases, so directing both the constancy and discrepancy of genetic information. Replication of genome initiate with DNA template-dependent fusion of small primers of RNA. This preliminary phase in replication of DNA demarcated as de novo primer synthesis which is catalyzed by specified polymerases known as primases. Sixteen diverse DNA-synthesizing enzymes about human perspective are devoted to replication, reparation, mutilation lenience, and inconsistency of nuclear DNA. But in dissimilarity, merely one DNA polymerase has been called in mitochondria. It has been suggest that PrimPol is extremely acting the roles by re-priming DNA replication in mitochondria to permit an effective and appropriate way replication to be accomplished. Investigations from a numeral of test site have significantly amplified our appreciative of the role, recruitment and regulation of the enzyme during DNA replication. Though, we are simply just start to increase in value the versatile roles that play PrimPol in eukaryote.

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DNA Polymerase: Structural Homology, Conformational Dynamics, and the Effects of Carcinogenic DNA Adducts

Journal of Nucleic Acids ◽

10.4061/2010/457176 ◽

2010 ◽

Vol 2010 ◽

pp. 1-15 ◽

Cited By ~ 7

Author(s):

Richard G. Federley ◽

Louis J. Romano

Keyword(s):

Dna Replication ◽

Dna Polymerase ◽

Dna Adducts ◽

Structural Changes ◽

Dna Polymerases ◽

Conformational Dynamics ◽

Three Dimensional ◽

Structural Homology ◽

Human Right ◽

Selection Of

DNA replication is vital for an organism to proliferate and lying at the heart of this process is the enzyme DNA polymerase. Most DNA polymerases have a similar three dimensional fold, akin to a human right hand, despite differences in sequence homology. This structural homology would predict a relatively unvarying mechanism for DNA synthesis yet various polymerases exhibit markedly different properties on similar substrates, indicative of each type of polymerase being prescribed to a specific role in DNA replication. Several key conformational steps, discrete states, and structural moieties have been identified that contribute to the array of properties the polymerases exhibit. The ability of carcinogenic adducts to interfere with conformational processes by directly interacting with the protein explicates the mutagenic consequences these adducts impose. Recent studies have identified novel states that have been hypothesised to test the fit of the nascent base pair, and have also shown the enzyme to possess a lively quality by continually sampling various conformations. This review focuses on the homologous structural changes that take place in various DNA polymerases, both replicative and those involved in adduct bypass, the role these changes play in selection of a correct substrate, and how the presence of bulky carcinogenic adducts affects these changes.

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