2018
DOI: 10.1016/j.dib.2018.02.081
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Data set on G4 DNA interactions with human proteins

Abstract: Guanine-rich DNA/RNA fragments can fold into G-quadruplexes (G4s) – non-canonical four-strand secondary structures. The article contains data on quadruplex interaction with human proteins. Binding of three topologically different G4 structures to more than 9000 human proteins was analyzed. Physicochemical methods were used to verify the results.The dataset was generated to identify the protein targets for DNA quadruplex structures for the purpose of better understanding the role of the structures in gene expre… Show more

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Cited by 13 publications
(20 citation statements)
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“…In the human protein microarray (protoarray) assay, [104] three topologically different model G4s were used. Top protein hits for all three or two of the three G4s included the following: ASXL1, a component of the polycomb complex PR-DUB (a histone deubiquitinase that mediates polycomb-target repression [105] ); the linker histone analogs HMGN1 and HMGN3, which modulate histone acetylation; [91,106,107] the linker histone analog HMGB2, which acts similarly to the above-mentioned HMGB1 but also participates in the demarcation of topologically associated chromatin domains by preventing aggregation of CCCTC-binding factor (CTCF); [108] the peptidylarginine deiminase 4 (PADi4), which mediates histone citrullination; [109] histone chaperones FACT (facilitates chromatin transcription) and BRD3 (bromodomain protein 3).…”
Section: G4s Might Directly Engage Architectural Chromatin Proteins mentioning
confidence: 99%
See 1 more Smart Citation
“…In the human protein microarray (protoarray) assay, [104] three topologically different model G4s were used. Top protein hits for all three or two of the three G4s included the following: ASXL1, a component of the polycomb complex PR-DUB (a histone deubiquitinase that mediates polycomb-target repression [105] ); the linker histone analogs HMGN1 and HMGN3, which modulate histone acetylation; [91,106,107] the linker histone analog HMGB2, which acts similarly to the above-mentioned HMGB1 but also participates in the demarcation of topologically associated chromatin domains by preventing aggregation of CCCTC-binding factor (CTCF); [108] the peptidylarginine deiminase 4 (PADi4), which mediates histone citrullination; [109] histone chaperones FACT (facilitates chromatin transcription) and BRD3 (bromodomain protein 3).…”
Section: G4s Might Directly Engage Architectural Chromatin Proteins mentioning
confidence: 99%
“…[114,115] BRD3 facilitates the transcription of hyperacetylated chromatin [116] and, along with other BET proteins (BRD2 and BRD4), is currently in the limelight with respect to epigenetic therapy (Box 1). Of the several BRD proteins analyzed in the protoarray assay, [104] BRD3 was the only candidate for efficient interaction with G4s (BRD4 and BRD2 were not tested). However, for the accurate evaluation of the binding affinities, future studies are required because protoarray profiling is a semiquantitative method.…”
Section: G4s Might Directly Engage Architectural Chromatin Proteins mentioning
confidence: 99%
“…Thus, CTCF recruitment to D regulated via several interlinked pathways (Figure 1), and G4s may contribute to e them. G4s affect methylation via sequestering DNA methyltransferase DNMT1 fro target sites [4] and may promote chromatin remodeling due to their affinit architectural chromatin proteins and modifiers, including polycomb related comp subunits [18,19]. This study was designed to partially verify the links between G4s, CGIs, chro compactness and CTCF recruitment.…”
Section: Introductionmentioning
confidence: 99%
“…Somewhat in line with these studies a large scale screening for G4 structure interacting factors using protein microarrays comprising >9000 human proteins found several factors that are involved in binding nucleosomes [126]. It is also likely that function of the G4 structure helicases like FANCJ [127], BLM [128], WRN [129], and REV-1 [49] would be important in epigenetic modifications in a replication-dependent manner (as demonstrated for REV-1) [49].…”
Section: Promise Of G4 Structure Binding Molecules In Epigenetics mentioning
confidence: 86%