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Literature summary for 5.6.2.4 extracted from

  • Chojnacki, M.; Melendy, T.
    The human papillomavirus DNA helicase E1 binds, stimulates, and confers processivity to cellular DNA polymerase epsilon (2018), Nucleic Acids Res., 46, 229-241 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.4

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of MBP-tagged helicase E1 (HPV 11 EE-E1) in High Five insect cells using the baculovirus expression system, recombinant expression of MBP-tagged enzyme and of GST-tagged in Escherichia coli human papillomavirus 11

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required human papillomavirus 11

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O human papillomavirus 11
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 ADP + phosphate
-
 ?
additional information human papillomavirus 11 DNA replicase E1 is conferring processivity to cellular DNA polymerase epsilon by directly tethering pol epsilon to the DNA parental strand and towing epsilon behind the E1 helicase as the replication fork progresses. The stimulation of pol epsilon by PV E1 is helicase-specific and dependent on ATP hydrolysis ?
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Organism

Organism UniProt Comment Textmining
human papillomavirus 11 P04014
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant HPV 11 EE-E1 from High Five insect cells by anion exchange chromatography, immunoaffinity chromatography on an anti-EE monoclonal antibody-protein A resin, and ultrafiltration. Recombinant MBP-tagged enzyme from Escherichia coli by amylose affinity chromatography. Recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography human papillomavirus 11

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 human papillomavirus 11 ADP + phosphate
-
 ?
ATP + H2O radioactive enzyme activity assay with gamma-32P-ATP human papillomavirus 11 ADP + phosphate
-
 ?
additional information DNA replicase E1 is conferring processivity to cellular DNA polymerase epsilon by directly tethering pol epsilon to the DNA parental strand and towing epsilon behind the E1 helicase as the replication fork progresses. The stimulation of pol epsilon by PV E1 is helicase-specific and dependent on ATP hydrolysis human papillomavirus 11 ?
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additional information HPV E1 physically interacts with DNA polymerases epsilon and delta. The stimulation of pol epsilon by PV E1 is helicase-specific and dependent on ATP hydrolysis. HPV E1 does not stimulate Escherichia coli DNA polymerase I or human pol delta human papillomavirus 11 ?
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Synonyms

Synonyms Comment Organism
DNA helicase E1
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 human papillomavirus 11
E1
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 human papillomavirus 11
HPV 11 EE-E1
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 human papillomavirus 11
HPV E1
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 human papillomavirus 11
HPV type 11
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 human papillomavirus 11
human papillomavirus DNA helicase
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 human papillomavirus 11
PVE1 helicase
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 human papillomavirus 11

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 ATPase assay at human papillomavirus 11

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 ATPase assay at human papillomavirus 11

General Information

General Information Comment Organism
evolution the enzyme demonstrates a unique capacity of a viral helicase having evolved to stimulate a cellular replicative DNA polymerase human papillomavirus 11
physiological function the human papillomavirus DNA helicase E1 binds, stimulates, and confers processivity to cellular DNA polymerase epsilon. The papillomavirus (PV) helicase protein E1 recruits components of the cellular DNA replication machinery to the PV replication fork, such as replication protein A (RPA), DNA polymerase alpha-primase (polalpha) and topoisomerase I (topo I). E1 binds to DNA polymerase epsilon (pol epsilon) and dramatically stimulates the DNA synthesis activity of pol epsilon. This stimulation of pol epsilon by E1 is highly specific and occurs even in the absence of the known pol epsilon cofactors replication Factor C (RFC), proliferating cell nuclear antigen (PCNA) and RPA. This stimulation is due to an increase in the processivity of pol epsilon and occurs independently of pol epsilon's replication cofactors. The increase in processivity is dependent on the ability of the E1 helicase to hydrolyze ATP, suggesting it is dependent on E1's helicase action. RPA is dispensable for processive synthesis by pol epsilon in the presence of E1. HPV E1 does not stimulate Escherichia coli DNA polymerase I or human pol delta human papillomavirus 11