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Central European Institute of Technol... 1 Centre for Advanced Materials Applica... 1 Department of Chemistry McGill Univer... 1 Institute of Biophysics Czech Academy... 1 Instituto de Química Física 'Blas Cab... 1 Laboratoire d'Optique and Biosciences... 1 National Centre for Biomolecular Rese... 1 Pharmaceutical and Pharmacological Sc... 1 Slovenian NMR Centre National Institu... 1
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Central European Institute of Technol... 1 Centre for Advanced Materials Applica... 1 Department of Chemistry McGill Univer... 1 Institute of Biophysics Czech Academy... 1 Instituto de Química Física 'Blas Cab... 1 Laboratoire d'Optique and Biosciences... 1 National Centre for Biomolecular Rese... 1 Pharmaceutical and Pharmacological Sc... 1 Slovenian NMR Centre National Institu... 1
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Free Medical Journals od 2010
Nature Open Access od 2010-12-01
PubMed Central od 2012
Europe PubMed Central od 2012
ProQuest Central od 2010-01-01
Open Access Digital Library od 2015-01-01
Open Access Digital Library od 2015-01-01
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PubMed
38443388
DOI
10.1038/s41467-024-46221-y
Knihovny.cz E-zdroje
I-Motifs (iM) are non-canonical DNA structures potentially forming in the accessible, single-stranded, cytosine-rich genomic regions with regulatory roles. Chromatin, protein interactions, and intracellular properties seem to govern iM formation at sites with i-motif formation propensity (iMFPS) in human cells, yet their specific contributions remain unclear. Using in-cell NMR with oligonucleotide iMFPS models, we monitor iM-associated structural equilibria in asynchronous and cell cycle-synchronized HeLa cells at 37 °C. Our findings show that iMFPS displaying pHT < 7 under reference in vitro conditions occur predominantly in unfolded states in cells, while those with pHT > 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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- azidy * MeSH
- benzazepiny * MeSH
- DNA MeSH
- HeLa buňky MeSH
- lidé MeSH
- magnetická rezonanční tomografie * MeSH
- protilátky MeSH
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