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ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2 [DNA-Seq validation of KO]

ABSTRACT: In order to investigate changes upon ZBTB10 depletion, we used CRISPR/Cas9 to induce a ZBTB10 knockout in HEK293 and U2OS cells.

ORGANISM(S): Homo sapiens

PROVIDER: GSE117213 | GEO | 2018/12/16

REPOSITORIES: GEO

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ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2 [RNA-Seq]

Project description:To study if ZBTB10 influences gene expression, we used CRISPR/Cas9 knockout HEK293 and U2OS cells to compare transcript levels between WT and KO.

2018-12-16 | GSE117212 | GEO

ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2

Project description:Telomeres are the ends of linear chromosomes and together with the shelterin complex present an essential feature for genome integrity. Vertebrate telomeres usually consist of hexameric TTAGGG repeats, however, in cells that use the alternative lengthening of telomeres (ALT) mechanism, variant repeat sequences are interspersed throughout telomeres. Previously, it was shown that NR2C/F transcription factors bind to TCAGGG variant repeats and contribute to telomere maintenance in ALT cells. While specific binders to other variant repeat sequences have been lacking to date, we here identify ZBTB10 as the first TTGGGG-binding protein and demonstrate direct binding via the two zinc fingers with affinity in the nanomolar range. Concomitantly, ZBTB10 co-localizes with a subset of telomeres in ALT-positive U2OS cells and interacts with TRF2/RAP1 via the N-terminal region of TRF2. Our data establishes ZBTB10 as a novel variant repeat-specific binding protein at ALT telomeres.

2018-12-17 | PXD010672 | Pride

ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2.

Project description:Telomeres are nucleoprotein structures at the ends of linear chromosomes and present an essential feature for genome integrity. Vertebrate telomeres usually consist of hexameric TTAGGG repeats, however, in cells that use the alternative lengthening of telomeres (ALT) mechanism, variant repeat sequences are interspersed throughout telomeres. Previously, it was shown that NR2C/F transcription factors bind to TCAGGG variant repeats and contribute to telomere maintenance in ALT cells. While specific binders to other variant repeat sequences have been lacking to date, we here identify ZBTB10 as the first TTGGGG-binding protein and demonstrate direct binding via the two zinc fingers with affinity in the nanomolar range. Concomitantly, ZBTB10 co-localizes with a subset of telomeres in ALT-positive U2OS cells and interacts with TRF2/RAP1 via the N-terminal region of TRF2. Our data establishes ZBTB10 as a novel variant repeat binding protein at ALT telomeres.

| S-EPMC6393293 | biostudies-literature

ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2

Project description:This SuperSeries is composed of the SubSeries listed below.

2018-12-16 | GSE117214 | GEO

ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2 [DNA-Seq validation of KO]

Project description:ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2 [DNA-Seq validation of KO]

| PRJNA481472 | ENA

ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2

Project description:ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2

| PRJNA481468 | ENA

ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2 [RNA-Seq]

Project description:ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2 [RNA-Seq]

| PRJNA481471 | ENA

An intramolecular G-quadruplex structure is required for binding of telomeric repeat-containing RNA to the telomeric protein TRF2.

Project description:Telomeric repeat-containing RNA (TERRA) is important for telomere regulation, but the structural basis for how TERRA localizes to chromosome ends is unknown. Here we report on studies exploring whether the TERRA G-quadruplex structure is critical for binding to telomeres. We demonstrate that the telomeric protein TRF2 binds TERRA via interactions that necessitate the formation of a G-quadruplex structure rather than the TERRA sequence per se. We also show that TRF2 simultaneously binds TERRA and telomeric duplex or G-quadruplex DNA. These observations suggest that the TERRA G-quadruplex is a key feature of telomere organization.

| S-EPMC3528108 | biostudies-literature

Cyclic Peptidic Mimetics of Apollo Peptides Targeting Telomeric Repeat Binding Factor 2 (TRF2) and Apollo Interaction.

Project description:Telomeric repeat binding factor 2 (TRF2) is a telomere-associated protein that plays an important role in the formation of the 3' single strand DNA overhang and the "T loop", two structures critical for the stability of the telomeres. Apollo is a 5'-exonuclease recruited by TRF2 to the telomere and contributes to the formation of the 3' single strand DNA overhang. Knocking down of Apollo can induce DNA damage response similar to that caused by the knocking down of TRF2. In this Letter, we report the design and synthesis of a class of cyclic peptidic mimetics of the TRFH binding motif of Apollo (ApolloTBM). We found conformational control of the C terminal residues of ApolloTBM can effectively improve the binding affinity. We have obtained a crystal structure of a cyclic peptidic Apollo peptide mimetic (34) complexed with TRF2, which provides valuable guidance to the future design of TRF2 inhibitors.

| S-EPMC5949732 | biostudies-literature

POT-3 preferentially binds the terminal DNA-repeat on the telomeric G-overhang.

Project description:Eukaryotic chromosomes typically end in 3' telomeric overhangs. The safeguarding of telomeric single-stranded DNA overhangs is carried out by factors related to the protection of telomeres 1 (POT1) protein in humans. Of the three POT1-like proteins in Caenorhabditis elegans, POT-3 was the only member thought to not play a role at telomeres. Here, we provide evidence that POT-3 is a bona fide telomere-binding protein. Using a new loss-of-function mutant, we show that the absence of POT-3 causes telomere lengthening and increased levels of telomeric C-circles. We find that POT-3 directly binds the telomeric G-strand in vitro and map its minimal DNA binding site to the six-nucleotide motif, GCTTAG. We further show that the closely related POT-2 protein binds the same motif, but that POT-3 shows higher sequence selectivity. Crucially, in contrast to POT-2, POT-3 prefers binding sites immediately adjacent to the 3' end of DNA. These differences are significant as genetic analyses reveal that pot-2 and pot-3 do not function redundantly with each other in vivo. Our work highlights the rapid evolution and specialisation of telomere binding proteins and places POT-3 in a unique position to influence activities that control telomere length.

| S-EPMC9881156 | biostudies-literature

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