1998
DOI: 10.1074/jbc.273.33.21332
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DNA Polymerase II (ε) of Saccharomyces cerevisiaeDissociates from the DNA Template by Sensing Single-stranded DNA

Abstract: Two forms of DNA polymerase II (⑀) of Saccharomyces cerevisiae, Pol II* and Pol II, were purified to near homogeneity from yeast cells. Pol II* is a four-subunit complex containing a 256-kDa catalytic polypeptide, whereas Pol II consists solely of a 145-kDa polypeptide derived from the N-terminal half of the 256-kDa polypeptide of Pol II*. We show that Pol II* and Pol II are indistinguishable with respect to the processivity and rate of DNA-chain elongation. The equilibrium dissociation constants of the comple… Show more

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Cited by 25 publications
(47 citation statements)
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“…Asturias et al (2006) suggest that this Dpb tail domain contributes directly to Pol e processivity by mediating engagement of Pol e with the DNA template, either instead of or in addition to the polymerase clamp, PCNA. This model is consistent with the observation that the processivity of the intact, four-subunit Pol e is higher than processivity of a 140-kDa N-terminal fragment of Pol2p, which lacks the Dpb subunits Maki et al 1998). The influence of proteins responsible for DNA polymerase processivity on fidelity of DNA synthesis has been tested (mainly in vitro, using primer extension assays) in several laboratories.…”
Section: Discussionsupporting
confidence: 66%
“…Asturias et al (2006) suggest that this Dpb tail domain contributes directly to Pol e processivity by mediating engagement of Pol e with the DNA template, either instead of or in addition to the polymerase clamp, PCNA. This model is consistent with the observation that the processivity of the intact, four-subunit Pol e is higher than processivity of a 140-kDa N-terminal fragment of Pol2p, which lacks the Dpb subunits Maki et al 1998). The influence of proteins responsible for DNA polymerase processivity on fidelity of DNA synthesis has been tested (mainly in vitro, using primer extension assays) in several laboratories.…”
Section: Discussionsupporting
confidence: 66%
“…A role for pol ⑀ in DNA replication late in S phase would also be consistent with the involvement of pol ⑀ in the response to DNA damage in S. cerevisiae (32,35). Different replication machinery may invoke different checkpoint responses depending on where in S phase a replication block or DNA damage is sensed.…”
Section: Discussionmentioning
confidence: 56%
“…These mutants also die rapidly when DNA replication is inhibited by hydroxyurea because they are defective in the ability to block mitosis in response to replication stress (33); although at least for mec1 and rad53 mutants, this inviability in hydroxyurea is a result of the inability to complete replication rather than inappropriate anaphase entry (34). In vitro, the pol ⑀ holoenzyme dissociates from its DNA template upon the addition of single-stranded DNA (35), suggesting a mechanism for how pol ⑀ is able to sense DNA damage or replication blocks. S. pombe pol ⑀ may indirectly participate in the DNA damage response through an interaction with cid1 ϩ .…”
mentioning
confidence: 99%
“…Something in the structure of the DNA itself, such as stretches of single-stranded DNA formed during replication and blocks due to DNA damage, has been proposed to act as a signal in the S phase, and the zinc finger of pol ⑀ has been proposed to monitor the signal (9). Single-stranded DNA has been shown to act both as an efficient trap for pol ⑀ and to actually promote dissociation of full-length pol ⑀ but not a pol ⑀ protein missing amino acids 1270 to the end (aa 2222) from primer-templates, suggesting that there is a binding site for single-stranded DNA in the large, non-catalytic C-terminal region (39). The mutant phenotypes described in this work suggest that the zinc finger region may be what is critical for single-stranded DNA sensing in that C-terminal segment.…”
Section: Mutations In Zf1 and Between Zf1 And Zf2 Show Reduced Inducimentioning
confidence: 99%