Herpesviral helicase-primase subunit UL8 is inactivated B-family polymerase

Kazlauskas, Darius; Venclovas, C̆eslovas

doi:10.1093/bioinformatics/btu204

Cited by 13 publications

(18 citation statements)

References 37 publications

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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%

“…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%

“…The helicase could be assigned to the helicase superfamily 1B (SF1B) [18] based on sequence [19] and 5 0 -3 0 directionality [20]. Recently, a bioinformatics analysis [21] related the helicase UL5 to the family of Pif1 helicases in contradiction with a previous assignment of the herpesvirus helicases to the Dda helicase family as proposed by Thierry et al [22]. Sequence conservation of the accessory protein between a-, b-and cherpesviruses is very low and was supposed to be limited to a central domain within the protein [23].…”

Section: Introductionmentioning

confidence: 99%

“…Sequence conservation of the accessory protein between a-, b-and cherpesviruses is very low and was supposed to be limited to a central domain within the protein [23]. Kazlauskas and Venclovas proposed that at least the C-terminal half of the accessory factor UL8 from a-herpesviruses corresponds to an inactive family B DNA polymerase [21]. But even for the best studied system, HSV, structural aspects of the helicase-primase complex remain elusive, but of high interest as it is targeted by the anti-HSV drugs Pritelivir and Amenamevir which progressed recently into phase II clinical trials (see James et al (24) for a recent review).…”

Section: Introductionmentioning

confidence: 99%

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Production and characterisation of Epstein–Barr virus helicase–primase complex and its accessory protein BBLF2/3

et al. 2015

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The helicase-primase complex is part of the lytic DNA replication machinery of herpesviruses, but up to now, almost nothing is known about its structure. For Epstein-Barr virus it consists in the helicase BBLF4, the primase BSLF1 and the accessory protein BBLF2/3. The accessory protein shows only weak sequence homology within the herpesvirus family but may be related to an inactive B-family polymerase. BSLF1 belongs to the archaeo-eukaryotic primase family, whereas the helicase BBLF4 has been related either to Dda helicases of caudovirales or to Pif1 helicases. We produced the helicase-primase complex in insect cells using a baculovirus coding for all three proteins simultaneously. The soluble monomeric helicase-primase complex containing the three proteins with 1:1:1 stoichiometry showed ATPase activity, which is strongly stimulated in the presence of ssDNA oligomers. Furthermore, we expressed BBLF2/3 as soluble monomeric protein and performed small-angle X-ray scattering experiments which yielded an envelope whose shape is compatible with B-family polymerases.

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Section: Bioinformatics Analysis Of Bblf2/3supporting

confidence: 72%

Section: Motifmentioning

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Production and characterisation of Epstein–Barr virus helicase–primase complex and its accessory protein BBLF2/3

et al. 2015

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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%

Fusion of a superfamily 1 helicase and an inactivated DNA polymerase is a signature of common evolutionary history of Polintons, polinton-like viruses, Tlr1 transposons and transpovirons

2016

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Polintons (polintoviruses), polinton-like viruses (PLVs) and virophages belong to a recently described major class of eukaryotic viruses that is characterized by a distinct virion morphogenetic protein module and, in many members, a protein-primed family B DNA polymerase (pDNAP). All Polintons, by definition, encode a pDNAP and a retrovirus-like integrase. Most of the PLV lack these genes and instead encode a large protein containing a superfamily 1 (SF1) helicase domain. We show here that the SF1 helicase domain-containing proteins of the PLV also contain an inactivated pDNAP domain. This unique helicase-pDNAP fusion is also encoded by transpovirons, enigmatic plasmid-like genetic elements that are associated with giant viruses of the family Mimiviridae. These findings indicate the directionality of evolution of different groups of viruses and mobile elements in the Polinton-centered class. We propose that the PLV evolved from a polinton via fusion of the pDNAP gene with a helicase gene that was accompanied by mutations in the pDNAP active site, likely resulting in inactivation of the polymerase activity. The transpovirons could have evolved from PLV via the loss of several genes including those encoding the morphogenetic module proteins. These findings reaffirm the central evolutionary position of the Polintons in the evolution of eukaryotic viruses and other mobile genetic elements.

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Comparative chloroplast genome analysis of four Hippophae rhamnoides subspecies and its phylogenetic analysis

Wang,

Liu

et al. 2023

Genet Resour Crop Evol

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Sea buckthorn(Hippophae rhamnoides), a hardy deciduous shrub of the family Elaeagnaceae, grows wild at high altitudes in Asia and Europe and is known for its great nutritional, medicinal and ecological value.In this study, the chloroplast genomesof four H. rhamnoidessubspecies, H. rhamnoides subsp. mongolica 'wulanshalin', H. rhamnoides subsp. caucasia, H. rhamnoides subsp. sinensis 'wucixiong', and H. rhamnoides subsp. yunnanensis, were characterized. The results showed that the genome length of these four subspecies ranged from 157,436 bp to 157,822 bp, with a typical quadripartite structure. Comparing the genome structure of these four subspecies, it was found that the chloroplast genomes were relatively conserved, retaining the same gene order. The annotation contained a total of 132 genes in each chloroplast genomes genome, with 86 protein-coding genes, 38 tRNA genes, and 8 rRNA genes. This study identi ed 14 highly differentiated regions and 423 simple sequence repeats loci, which can be used as potential molecular markers for H. rhamnoides. Meanwhile, Phylogenetic analysis showed that all Hippophae taxa were clustered in the same group and formed a sister clade with Elaeagnus taxa supported by Bayesian posterior probabilities. Among Hippophae taxa, H. gyantsensis, H. neurcar and H. salicifolia were grouped together, but H. tibetana was clustered with H. rhamnoide and the other six H. rhamnoide subspecies. The ndings of this research will be useful for further studies on resource protection and the taxonomic classi cation of sea buckthorn.

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Herpesviral helicase-primase subunit UL8 is inactivated B-family polymerase

Abstract: Supplementary data are available at Bioinformatics online.

Cited by 13 publications

References 37 publications

Production and characterisation of Epstein–Barr virus helicase–primase complex and its accessory protein BBLF2/3

Production and characterisation of Epstein–Barr virus helicase–primase complex and its accessory protein BBLF2/3

Fusion of a superfamily 1 helicase and an inactivated DNA polymerase is a signature of common evolutionary history of Polintons, polinton-like viruses, Tlr1 transposons and transpovirons

Comparative chloroplast genome analysis of four Hippophae rhamnoides subspecies and its phylogenetic analysis

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