2014
DOI: 10.1093/bioinformatics/btu204
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Herpesviral helicase-primase subunit UL8 is inactivated B-family polymerase

Abstract: Supplementary data are available at Bioinformatics online.

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Cited by 14 publications
(18 citation statements)
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“…6c). The shape of the envelope obtained by SAXS resembled the one from vaccinia virus polymerase E9 [40] which meant that it was indeed compatible with a structure related to family B polymerases as proposed by Kazlauskas and Venclovas [21]. Using the model of the polymerase from T. gorgonarius [41], chosen because of the similar number of residues, a reasonable fit into the SAXS envelope (Fig.…”
Section: Bioinformatics Analysis Of Bblf2/3supporting
confidence: 72%
See 3 more Smart Citations
“…6c). The shape of the envelope obtained by SAXS resembled the one from vaccinia virus polymerase E9 [40] which meant that it was indeed compatible with a structure related to family B polymerases as proposed by Kazlauskas and Venclovas [21]. Using the model of the polymerase from T. gorgonarius [41], chosen because of the similar number of residues, a reasonable fit into the SAXS envelope (Fig.…”
Section: Bioinformatics Analysis Of Bblf2/3supporting
confidence: 72%
“…The residue required for DNA replication (mutant A23, [46]) maps into the conserved motif 1 and the one important for interaction with UL52 (mutant A49, [46]) to motif 4. As it has been proposed very recently that aherpesvirus accessory proteins might be related to family B polymerases [21], this might also be true for BBLF2/3 and herpesvirus accessory proteins in general. The envelope for BBLF2/3 which we obtained from the SAXS data with its oblate shape and its characteristic central depression agrees well with the high-resolution structure of B polymerases (Fig.…”
Section: Motifmentioning
confidence: 87%
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“…Inactivated family B DNAP domains have been detected previously, in particular in the eukaryotic DNA polymerase ε (Tahirov et al 2009), in a distinct family of archaeal DNAP homologs (Rogozin et al 2008; Makarova et al 2014), in a poxvirus virion protein (Yutin et al 2014) and in one of the subunits of the herpesvirus helicase-primase complex (Kazlauskas and Venclovas 2014). The biological functions of these inactivated DNAP homologs have not been studied in detail but they are predicted to play structural roles in replisomes and beyond (Tahirov et al 2009; Kazlauskas and Venclovas 2014; Yutin et al 2014).…”
Section: Resultsmentioning
confidence: 99%