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Details on Person HHV8 single-stranded DNA binding protein (DBP, ORF6) coats s...

Class:IdSummation:9991225
_displayNameHHV8 single-stranded DNA binding protein (DBP, ORF6) coats s...
_timestamp2026-06-04 16:46:28
created[InstanceEdit:9991213] Stephan, Ralf, 2026-06-04
textHHV8 single-stranded DNA binding protein (DBP, ORF6) coats ssDNA exposed at ori-Lyt during lytic replication by binding cooperatively along the strand and assembling into a regular nucleoprotein filament; electron microscopy of recombinant DBP incubated with M13 ssDNA showed uniform filaments 9 nm in width with a 7.3 nm axial repeat in which the ssDNA secondary structure is disrupted and extended to ~0.28 nm per nucleotide, with each monomer covering roughly 22 nt, while a C-terminal truncation abolished cooperative coating, indicating that oligomerisation through the C-terminus drives filament propagation along the strand (Ozgur and Griffith, 2014). DBP also self-assembles into long double-helical protein filaments in the absence of DNA that can engulf ssDNA tails of partially duplex substrates without disruption, suggesting that pre-formed DBP scaffolds can take up unwound ssDNA at replication compartments (Ozgur et al. 2011). Genetic deletion of DBP from the HHV8 BAC abolishes ori-Lyt-dependent lytic DNA synthesis and infectious virion production, defects rescued by DBP supplied in trans, establishing that this ssDNA-coating activity is essential for viral lytic replication (Peng et al. 2014).
(summation)[BlackBoxEvent:9991233] DBP coats unwound ssDNA [Homo sapiens]
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