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Biology subjects

Bonnet, H.

Publications and source records attributed to Bonnet, H..

3 recordsLinked to original sources

Molecular characterization of flower bud dormancy under constrained temperatures unveils a shallow dormancy stage induced by cold deprivation

Mild winters are becoming increasingly common in temperate regions due to climate change, which may have important impacts on ecosystems and agriculture. In particular, rising temperatures affect the progression of winter dormancy--a crucial developmental stage in perennial plants--making tree development and reproduction particularly vulnerable to climate change. A better understanding of how future temperature conditions will disrupt dormancy in cultivated fruit trees is crucial for anticipating the impeding consequences and identifying potential adaptation strategies. We investigated the effect of very constrained temperature conditions, i.e. several levels of cold deprivation and early cold exposure, on sweet cherry flower buds during dormancy onset and maintenance, using phenological observations and transcriptomic analyses. We show that temperature is a major driver of dormancy progression as cold deprivation and early cold exposure strongly modify the timing of phenological phases as well as gene expression patterns. We identified genes and signaling pathways specifically activated and/or repressed by cold temperatures, and therefore potentially involved in the optimal progression of dormancy. Finally, thanks to an integrative analysis of molecular data obtained under natural and prolonged warm conditions, we characterize a distinct shallow dormancy phase induced by cold deprivation, with a unique molecular signature. HighlightsOur phenological and molecular analysis of sweet cherry dormancy under constrained conditions reveals a gene expression timeline in response to temperature and uncovers a shallow dormancy stage induced by cold deprivation.

plant biology↗

Antibody targeting the anti-parallel topology of human telomeric G-quadruplex DNA

G-quadruplexes (G4s) are four-stranded nucleic acid structures that have gathered a significant attention due to their involvement in key biological processes, including gene regulation, genome stability, and telomeres maintenance. Some G4 antibodies have been developed to selectively recognize these structures over duplex DNA; however, most, even the widely studied BG4 and 1H6, bind G4s in a general manner and lack discrimination between distinct topologies, particularly between parallel and antiparallel conformations. In this study, we report on the development and characterization of a novel antibody selected via phage display method using a constrained antiparallel G4 structure mimicking one of the conformation adopted in vitro by the human telomeric sequence. Our findings demonstrate that this new antibody selectively recognizes the antiparallel topology of the telomeric G4 sequence, a property further validated in cellular models.

biochemistry↗

iMab Antibody Binds Single-Stranded Cytosine-Rich Sequences and Unfolds DNA i-Motifs

i-Motifs (iMs) are non-canonical, four-stranded secondary structures formed by stacking of hemi-protonated CH+{middle dot}C base pairs in cytosine-rich DNA sequences, predominantly at pH < 7. The presence of iM structures in cells was a matter of debate until the recent development of iM-specific antibody, iMab, that was instrumental for several studies that suggested the existence of iMs in live cells and their putative biological roles. We assessed the interaction of iMab with cytosine-rich oligonucleotides by biolayer interferometry (BLI), pull-down assay and bulk-FRET experiments. Our results suggest that binding of iMab to DNA oligonucleotides is governed by the presence of runs of at least two consecutive cytosines and is generally increased in acidic conditions, irrespectively of the capacity of the sequence to adopt, or not, an iM structure. Moreover, the results of the bulk-FRET assay indicate that interaction with iMab results in unfolding of iM structures even in acidic conditions (pH 5.8 or 6.5), similarly to what has been observed with hnRNP K, well-studied single- stranded DNA binding protein. Taken together, our results suggest that iMab actually binds to blocks of 2-3 cytosines in single-stranded DNA, and call for more careful interpretation of results obtained with this antibody.

biophysics↗