| Dinoflagellate viral nucleoprotein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | DUF5756 | ||||||||
| Pfam | PF19060 | ||||||||
| |||||||||
Dinoflagellate/viral nucleoproteins (DVNPs) are a family of positively-charged, DNA-binding nucleoproteins found exclusively in dinoflagellates and Nucleocytoviricota. It serves to compact DNA in these organisms.
The proteins are known to pack DNA more tightly than histones do. When expressed in eukaryotes that possess histones, they displace nucleosomes and impair translation. This action is thought to be one of the driving forces for dinoflagellates to switch to this protein instead of histone for packaging. Some dinoflagellates have further switched to dinoflagellate histone-like proteins (HLPs) for packaging.
The version of DVNPs in dinoflagellates have a variable N-terminal tail with a nuclear localization signal. It also has many phosphorylation sites, a feature not seen in viral counterparts. The fixed C-terminal domain may have a helix-turn-helix fold.
References
- Hu II, Waller (March 2019). "The unorthodox chromosomal organisation of the dinoflagellates". Access Microbiology. 1 (1A). doi:10.1099/acmi.ac2019.po0119.
- Irwin NA, Martin BJ, Young BP, Browne MJ, Flaus A, Loewen CJ, et al. (April 2018). "Viral proteins as a potential driver of histone depletion in dinoflagellates". Nature Communications. 9 (1): 1535. doi:10.1038/s41467-018-03993-4. PMC 5906630. PMID 29670105.
- Riaz S, Sui Z, Niaz Z, Khan S, Liu Y, Liu H (December 2018). "Distinctive Nuclear Features of Dinoflagellates with A Particular Focus on Histone and Histone-Replacement Proteins". Microorganisms. 6 (4): 128. doi:10.3390/microorganisms6040128. PMC 6313786. PMID 30558155.
- Gornik SG, Ford KL, Mulhern TD, Bacic A, McFadden GI, Waller RF (December 2012). "Loss of nucleosomal DNA condensation coincides with appearance of a novel nuclear protein in dinoflagellates". Current Biology. 22 (24): 2303–12. doi:10.1016/j.cub.2012.10.036. PMID 23159597.