Show simple item record

dc.contributor.authorGarcía-Quintans, Nieves
dc.contributor.authorBaquedano, Ignacio
dc.contributor.authorBlesa, Alba
dc.contributor.authorVerdú, Carlos
dc.contributor.authorBerenguer, José
dc.contributor.authorMencía, Mario
dc.description.abstractPrimase-polymerases (Ppol) are one of the few enzymes able to start DNA synthesis on ssDNA templates. The role of Thermus thermophilus HB27 Ppol, encoded along a putative helicase (Hel) within a mobile genetic element (ICETh2), has been studied. A mutant lacking Ppol showed no effects on the replication of the element. Also, no apparent differences in the sensitivity to DNA damaging agents and other stressors or morphological changes in the mutant cells were detected. However, the mutants lacking Ppol showed an increase in two to three orders of magnitude in their transformation efficiency with plasmids and genomic DNA acquired from the environment (eDNA), independently of its origin and G + C content. In contrast, no significant differences with the wild type were detected when the cells received the DNA from other T. thermophilus partners in conjugation-like mating experiments. The similarities of this behaviour with that shown by mutants lacking the Argonaute (ThAgo) protein suggests a putative partnership Ppol-ThAgo in the DNA–DNA interference mechanism of defence, although other eDNA defence mechanisms independent of ThAgo cannot be
dc.publisherEnvironmental Microbiologyspa
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 España*
dc.titleA thermostable DNA primase-polymerase from a mobilegenetic element involved in defence againstenvironmental
dc.typejournal articlespa
dc.rights.accessRightsopen accessspa
dc.description.extent697 KBspa

Files in this item


This item appears in the following Collection(s)

Show simple item record

Atribución-NoComercial-SinDerivadas 3.0 España
Except where otherwise noted, this item's license is described as Atribución-NoComercial-SinDerivadas 3.0 España