A euryarchaeal histone modulates strand displacement synthesis by replicative DNA polymerases

Sun, Fei; Huang, Li

doi:10.1007/s11427-016-5076-8

Cited by 4 publications

(3 citation statements)

References 25 publications

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“…Both PabPolD and PabPolB can extend DNA primers, with PabPolD requiring PabPCNA for efficient DNA synthesis. PabPolD conversely exhibits DNA strand displacement activity in the absence of PabPCNA, but PabPolB requires PabPCNA for this activity [47,48], with strand displacement activity inhibited for both polymerases in P. furiosus by the HPfA1 histone protein [49]. Only PabPolD can extend RNA primers, with RNA strand displacement only occurring for PabPCNA-stimulated PabPolD [47], suggesting a role for PolD in initial extension of primed templates on both leading and lagging strands.…”

Section: Euryarchaeotal Replication: Current Statusmentioning

confidence: 99%

Archaeal DNA polymerases: new frontiers in DNA replication and repair

Cooper

2018

Emerging Topics in Life Sciences

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Archaeal DNA polymerases have long been studied due to their superior properties for DNA amplification in the polymerase chain reaction and DNA sequencing technologies. However, a full comprehension of their functions, recruitment and regulation as part of the replisome during genome replication and DNA repair lags behind well-established bacterial and eukaryotic model systems. The archaea are evolutionarily very broad, but many studies in the major model systems of both Crenarchaeota and Euryarchaeota are starting to yield significant increases in understanding of the functions of DNA polymerases in the respective phyla. Recent advances in biochemical approaches and in archaeal genetic models allowing knockout and epitope tagging have led to significant increases in our understanding, including DNA polymerase roles in Okazaki fragment maturation on the lagging strand, towards reconstitution of the replisome itself. Furthermore, poorly characterised DNA polymerase paralogues are finding roles in DNA repair and CRISPR immunity. This review attempts to provide a current update on the roles of archaeal DNA polymerases in both DNA replication and repair, addressing significant questions that remain for this field.

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Section: Euryarchaeotal Replication: Current Statusmentioning

confidence: 99%

Archaeal DNA polymerases: new frontiers in DNA replication and repair

Cooper

2018

Emerging Topics in Life Sciences

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“…8,9 In general, SDDS shows a lower processivity and rate compared with primer extension (PE). 10,11 Previous studies have revealed that high GC content 12,13 and protein binding 14,15 in the downstream duplex inhibits SDDS. Recently, our group has identified that DNA polymerase gp90 from Pseudomonas aeruginosa phage 1 (PaP1) is an A-family processive DNA polymerase containing 3′-5′ Exo activities.…”

Section: Introductionmentioning

confidence: 99%

DNA polymerase Gp90 activities and regulations on strand displacement DNA synthesis revealed at single‐molecule level

Zhang

Xiao

et al. 2021

FASEB j.

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Strand displacement DNA synthesis (SDDS) is an essential step in DNA replication.With magnetic tweezers, we investigated SDDS kinetics of wild-type gp90 and its exonuclease-deficient polymerase gp90 exoat single-molecule level. A novel binding state of gp90 to the fork flap was confirmed prior to SDDS, suggesting an intermediate in the initiation of SDDS. The rate and processivity of SDDS by gp90 exoor wt-gp90 are increased with force and dNTP concentration. The rate and processivity of exonuclease by wt-gp90 are decreased with force. High GC content decreases SDDS and exonuclease processivity but increases exonuclease rate for wt-gp90. The high force and dNTP concentration and low GC content facilitate the successive SDDS but retard the successive exonuclease for wt-gp90. Furthermore, increasing GC content accelerates the transition from SDDS or exonuclease to exonuclease. This work reveals the kinetics of SDDS in detail and offers a broader cognition on the regulation of various factors on SDDS at single-polymerase level.

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“…These histones appeared to act as the major chromatin protein by forming extended polymeric structures that wrap DNA in multiples of 30-60 bp. Like eukaryotic histones, in some species archaeal histones have been shown to influence global transcription levels by hindering initiation (15) or elongation (16). Archaeal histones can also inhibit the binding of site-specific transcription factors (TFs) through competition (17).…”

Section: Introductionmentioning

confidence: 99%

An archaeal histone-like protein regulates gene expression in response to salt stress

Sakrikar

Schmid

2021

Preprint

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Histones, ubiquitous in eukaryotes as DNA-packing proteins, find their evolutionary origins in archaea. Unlike the characterized histone proteins of a number of methanogenic and themophilic archaea, previous research indicated that HpyA, the sole histone encoded in the model halophile Halobacterium salinarum, is not involved in DNA packaging. Instead, it was found to have widespread but subtle effects on gene expression and to maintain wild type cell morphology; however, its precise function remains unclear. Here we use quantitative phenotyping, genetics, and functional genomic to investigate HpyA function. These experiments revealed that HpyA is important for growth and rod-shaped morphology in reduced salinity. HpyA preferentially binds DNA at discrete genomic sites under low salt to regulate expression of ion uptake, particularly iron. HpyA also globally but indirectly activates other ion uptake and nucleotide biosynthesis pathways in a salt-dependent manner. Taken together, these results demonstrate an alternative function for an archaeal histone-like protein as a transcriptional regulator, with its function tuned to the physiological stressors of the hypersaline environment.

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A euryarchaeal histone modulates strand displacement synthesis by replicative DNA polymerases

Cited by 4 publications

References 25 publications

Archaeal DNA polymerases: new frontiers in DNA replication and repair

Archaeal DNA polymerases: new frontiers in DNA replication and repair

DNA polymerase Gp90 activities and regulations on strand displacement DNA synthesis revealed at single‐molecule level

An archaeal histone-like protein regulates gene expression in response to salt stress

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