Alessandro Vannini
- Head of Structural Biology Research Centre, Biologia Strutturale
- Research Group Leader, Vannini Group
Alessandro Vannini è un biochimico. Dirige il Centro di Biologia Strutturale dopo quasi otto anni passati nel Regno Unito in qualità di Principal Investigator e Deputy Head of Division all’Institute of Cancer Research di Londra.
Il suo laboratorio si occupa di studiare in dettaglio i meccanismi molecolari di complessi proteici che vengono assemblati intorno a siti di legame per la RNA Polymerase III e che giocano un ruolo fondamentale nella regolazione dell’espressione genica e nella organizzazione strutturale del genoma eucariotico. Questi meccanismi sono spesso deregolati in patalogie umane, quali il cancro e malattie neurodegenerative congenite.
Email: alessandro.vannini[at]fht.org
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Pubblicazioni
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10/2020 - Biochemical Society Transactions
Condensin complexes: understanding loop extrusion one conformational change at a time
Condensin and cohesin, both members of the structural maintenance of chromosome (SMC) family, contribute to the regulation and structure of chromatin. Recent work has shown both condensin and cohesin extrude DNA loops and most likely work via a conserved mechanism. This review focuses on condensin complexes, highlighting recent in vitro work characterising DNA loop formation and protein […]
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07/2020 - Nature Metabolism
A micronutrient with major effects on cancer cell viability
Selenium is a micronutrient essential for the generation of selenoproteins, which function predominantly by detoxifying cellular reactive oxygen species. In this issue, Carlisle et al. describe a novel mechanism whereby perturbing selenium utilization via inhibition of SEPHS2, a component of the selenocysteine-biosynthesis pathway, results in selenide poisoning and cancer cell death.
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07/2020 - Molecular Cell
Human Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA
Structural maintenance of chromosomes (SMC) complexes are essential for genome organization from bacteria to humans, but their mechanisms of action remain poorly understood. Here, we characterize human SMC complexes condensin I and II and unveil the architecture of the human condensin II complex, revealing two putative DNA-entrapment sites. Using single-molecule imaging, we demonstrate that both […]
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06/2020 - Cell
Hybrid Gene Origination Creates Human-Virus Chimeric Proteins during Infection
RNA viruses are a major human health threat. The life cycles of many highly pathogenic RNA viruses like influenza A virus (IAV) and Lassa virus depends on host mRNA, because viral polymerases cleave 5′-m7G-capped host transcripts to prime viral mRNA synthesis (“cap-snatching”). We hypothesized that start codons within cap-snatched host transcripts could generate chimeric human-viral […]
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06/2020 - Nature Communications
DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability
The TATA-binding protein (TBP) and a transcription factor (TF) IIB-like factor are important constituents of all eukaryotic initiation complexes. The reason for the emergence and strict requirement of the additional initiation factor Bdp1 in the RNA polymerase (RNAP) III system, however, remained elusive. A poorly studied aspect in this context is the effect of DNA […]
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