Journal
FRONTIERS IN MOLECULAR BIOSCIENCES
Volume 7, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fmolb.2020.00219
Keywords
SR; RS motifs; SR protein kinases; coronaviruses; capsid assembly; disassembly; N protein
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Funding
- E1BM103 Program - European Union (European Social Fund - ESF) [MIS 5047934]
- Greek national funds through the Operational Program Human Resources Development, Education and Lifelong Learning 2014-2020
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SR/RS domains are found in almost all eukaryotic genomes fromC. elegansto human. These domains are thought to mediate interactions between proteins but also between proteins and RNA in complex networks associated with mRNA splicing, chromatin structure, transcription, cell cycle and cell structure. A precise and tight regulation of their function is achieved through phosphorylation of a number of serine residues within the SR/RS motifs by the Serine-Arginine protein kinases (SRPKs) that lead to delicate structural alterations. Given that coronavirus N proteins also contain SR/RS domains, we formulate the hypothesis that the viruses exploit the properties of these motifs to promote unpacking of viral RNA and virion assembly.
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