Publications by authors named "Christophe Cardone"
The phosphoprotein P of () is an essential co-factor of the viral RNA polymerase L. Its prime function is to recruit L to the ribonucleocapsid composed of the viral genome encapsidated by the nucleoprotein N. phosphoproteins often contain a high degree of disorder.
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- Phosphoproteins (P) are crucial components of viral polymerases, linking the catalytic subunit to the ribonucleoprotein template, featuring a conserved overall structure despite their diverse forms.
- *They are primarily small, multidomain proteins with an oligomerization domain that has a defined 3D structure, while most of their regions are intrinsically disordered, allowing flexibility in interactions.
- *P proteins facilitate viral transcription and replication by forming transient complexes with viral and cellular proteins, showcasing the structural adaptability of intrinsically disordered protein domains.
Respiratory syncytial virus (RSV) RNA synthesis occurs in cytoplasmic inclusion bodies (IBs) in which all the components of the viral RNA polymerase are concentrated. In this work, we show that RSV P protein recruits the essential RSV transcription factor M2-1 to IBs independently of the phosphorylation state of M2-1. We also show that M2-1 dephosphorylation is achieved by a complex formed between P and the cellular phosphatase PP1.
View Article and Find Full Text PDFPhosphoprotein is the main cofactor of the viral RNA polymerase of It is involved in multiple interactions that are essential for the polymerase function. Most prominently it positions the polymerase complex onto the nucleocapsid, but also acts as a chaperone for the nucleoprotein. phosphoproteins lack sequence conservation, but contain all large disordered regions.
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