J 2024

In-cell NMR suggests that DNA i-motif levels are strongly depleted in living human cells

VÍŠKOVÁ, Pavlína; Eva IŠTVÁNKOVÁ; Jan RYNEŠ; Šimon DŽATKO; Tomáš LOJA et. al.

Basic information

Original name

In-cell NMR suggests that DNA i-motif levels are strongly depleted in living human cells

Authors

VÍŠKOVÁ, Pavlína; Eva IŠTVÁNKOVÁ; Jan RYNEŠ; Šimon DŽATKO; Tomáš LOJA; Martina LENARČIČ ŽIVKOVIC; Riccardo RIGO; Roberto EL-KHOURY; Israel SERRANO-CHACON; Masad J DAMHA; Carlos GONZALEZ; Jean-Louis MERGNY; Silvie TRANTÍRKOVÁ and Lukáš TRANTÍREK

Edition

Nature Communications, London, Nature Publishing Group, 2024, 2041-1723

Other information

Language

English

Type of outcome

Article in a journal

Country of publisher

Germany

Confidentiality degree

is not subject to a state or trade secret

References:

Organization

Středoevropský technologický institut – Repository – Repository

UT WoS

001180394600033

EID Scopus

2-s2.0-85186873110

Keywords in English

CYTOSINE-RICH STRAND; G-QUADRUPLEX; HNRNP LL; MOLECULAR SWITCH; GENE-EXPRESSION; LOOP LENGTH; STABILITY; SEQUENCES; DOMAINS; PROTEIN

Links

EF18_046/0015974, research and development project. EF20_079/0017045, research and development project. GX19-26041X, research and development project. LM2023050, research and development project. LM2023053, research and development project. LX22NPO5102, research and development project. 871037, interní kód Repo. CIISB III, large research infrastructures. Czech-BioImaging III, large research infrastructures. EATRIS-CZ IV, large research infrastructures.
Changed: 15/3/2025 00:51, RNDr. Daniel Jakubík

Abstract

V originále

gt; 7 appear as a mix of folded and unfolded states depending on the cell cycle phase. Comparing these results with previous data obtained using an iM-specific antibody (iMab) reveals that cell cycle-dependent iM formation has a dual origin, and iM formation concerns only a tiny fraction (possibly 1%) of genomic sites with iM formation propensity. We propose a comprehensive model aligning observations from iMab and in-cell NMR and enabling the identification of iMFPS capable of adopting iM structures under physiological conditions in living human cells. Our results suggest that many iMFPS may have biological roles linked to their unfolded states.

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