Davide Tamborrini

ORCID: 0000-0002-7311-2973
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About
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Research Areas
  • Genomics and Chromatin Dynamics
  • Cardiomyopathy and Myosin Studies
  • Ubiquitin and proteasome pathways
  • Photosynthetic Processes and Mechanisms
  • Muscle Physiology and Disorders
  • Cardiovascular Effects of Exercise
  • Fungal and yeast genetics research
  • DNA Repair Mechanisms
  • RNA modifications and cancer
  • Microtubule and mitosis dynamics
  • Biofuel production and bioconversion
  • RNA and protein synthesis mechanisms
  • Epigenetics and DNA Methylation
  • Protein Degradation and Inhibitors

Max Planck Institute of Molecular Physiology
2018-2024

Centre de Recherche en Biologie cellulaire de Montpellier
2018-2019

Abstract The thick filament is a key component of sarcomeres, the basic units striated muscle 1 . Alterations in proteins are associated with familial hypertrophic cardiomyopathy and other heart diseases 2 Despite central importance filament, its molecular organization remains unclear. Here we present architecture native cardiac sarcomeres relaxed state, determined by cryo-electron tomography. Our reconstruction reveals three-dimensional myosin, titin myosin-binding protein C (MyBP-C)....

10.1038/s41586-023-06690-5 article EN cc-by Nature 2023-11-01

Abstract The thick filament is a key component of sarcomeres, the basic force-generating and load-bearing unit striated muscle 1 . Mutations in proteins are associated with familial hypertrophic cardiomyopathy other heart diseases 2, 3 Despite this central importance for sarcomere force generation, it remains unclear how filaments structurally organized its components interact each thin to enable highly regulated contraction. Here, we present molecular architecture native cardiac sarcomeres...

10.1101/2023.04.11.536387 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-04-11

Abstract In many eukaryotic organisms cytokinesis is driven by a contractile actomyosin ring (CAR) that guides membrane invagination. What triggers CAR constriction at precise time of the cell cycle fundamental question. budding yeast assembled via septin scaffold division site. A Hippo-like kinase cascade, Mitotic Exit Network (MEN), promotes mitotic exit and cytokinesis, but whether how these two processes are independently controlled MEN poorly understood. Here we show critical function...

10.1038/s41467-018-06767-0 article EN cc-by Nature Communications 2018-10-11

Chromatin remodeling complexes are multi-subunit nucleosome translocases that reorganize chromatin in the context of DNA replication, repair, and transcription. To understand how these find their target sites on chromatin, we use genetically encoded photo-cross-linker amino acids to map footprint Sth1, catalytic subunit RSC complex, nucleosomes living yeast. We H3 K14 acetylation induces interaction Sth1 bromodomain with tail mediates neighboring rather than recruiting it chromatin....

10.1016/j.isci.2020.101292 article EN cc-by-nc-nd iScience 2020-06-20

Abstract Chromatin remodelling complexes are multi-subunit nucleosome translocases that reorganize chromatin in the context of DNA replication, repair and transcription. A key question is how these find their target sites on chromatin. Here, we use genetically encoded photo-crosslinker amino acids to map footprint Sth1, catalytic subunit RSC (remodels structure chromatin) complex, living yeast. We interaction Sth1 bromodomain with H3 tail depends K14 acetylation by Gcn5. This modification...

10.1101/2020.03.02.972562 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2020-03-03

Chromatin remodelling complexes are multi-subunit nucleosome translocases that reorganize chromatin in the context of DNA replication, repair and transcription. A key question is how these find their target sites on chromatin. Here, we use genetically encoded photo-crosslinker amino acids to map footprint Sth1, catalytic subunit RSC (remodels structure chromatin) complex, living yeast. We interaction Sth1 bromodomain with H3 tail depends K14 acetylation by Gcn5. This modification does not...

10.2139/ssrn.3565020 article EN SSRN Electronic Journal 2020-01-01
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