Human homologues of yeast helicase

Lü, Jing; Mullen, Janet R.; Brill, Steven J.; Kleff, Susanne; Romeo, Annette M.; Sternglanz, Rolf

doi:10.1038/383678a0

Cited by 147 publications

(154 citation statements)

References 10 publications

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“…Furthermore, their respective protein level increases during S-phase (20,21) and the mutants are sensitive to hydroxyurea (HU), an inhibitor of ribonucleotide reductase that generates replicative defects (19,22). The Sgs1 and Srs2 proteins share no homology with each other, but they do unwind DNA with the same 3Ј to 5Ј polarity (23,24). Sgs1 belongs to the RecQ-type helicase subfamily and has several orthologues in mammalian cells.…”

mentioning

confidence: 99%

Alternate pathways involving Sgs1/Top3, Mus81/ Mms4, and Srs2 prevent formation of toxic recombination intermediates from single-stranded gaps created by DNA replication

Fabre

Chan

Heyer

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

298

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Toxic recombination events are detected in vegetative Saccharomyces cerevisiae cells through negative growth interactions between certain combinations of mutations. For example, mutations affecting both the Srs2 and Sgs1 helicases result in extremely poor growth, a phenotype suppressed by mutations in genes that govern early stages of recombination. Here, we identify a similar interaction involving double mutations affecting Sgs1 or Top3 and Mus81 or Mms4. We also find that the primary DNA structures that initiate these toxic recombination events cannot be double-strand breaks and thus are likely to be single-stranded DNA. We interpret our results in the context of the idea that replication stalling leaves single-stranded DNA, which can then be processed by two competing mechanisms: recombination and nonrecombination gap-filling. Functions involved in preventing toxic recombination would either avoid replicative defects or act on recombination intermediates. Our results suggest that Srs2 channels recombination intermediates back into the gap-filling route, whereas Sgs1/Top3 and Mus81/Mms4 are involved in recombination and/or in replication to allow replication restart

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mentioning

confidence: 99%

Alternate pathways involving Sgs1/Top3, Mus81/ Mms4, and Srs2 prevent formation of toxic recombination intermediates from single-stranded gaps created by DNA replication

Fabre

Chan

Heyer

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

298

360

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“…These results led the authors to suggest that, although it is dispensable for the catalytic activity of bacterial RecQ, the HRDC domain might facilitate the unwinding of long DNA duplexes by stably binding DNA . A HRDC truncation mutant of Sgs1 protein is also active as a helicase and ATPase in vitro (Bennett et al, 1998;Lu et al, 1996). Conversely, studies with a BLM mutant lacking the HRDC region demonstrated that, although this domain has a minor effect on forked-duplex unwinding and is not required for ATP hydrolysis, it does play an important role in Holliday junction disruption (Janscak et al, 2003;Wu et al, 2005).…”

Section: The Helicase-and-rnased-like-c-terminal Domainmentioning

confidence: 99%

RecQ helicases: Multiple structures for multiple functions?

Vindigni

Hickson

2009

HFSP Journal

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“…BLM belongs to a subfamily of RecQ-type DNA helicases that includes the Escherichia coli protein RecQ (Nakayama et al, 1985), Saccharomyces cerevisiae Sgs1 (Lu et al, 1996), Schizosaccharomyces pombe Rqh1/Hus2/Rad12, (Murray et al, 1997;Stewart et al, 1997) and the human proteins RecQL (Puranam and Blackshear, 1994;Seki et al, 1994), WRN, the protein mutated in Werner syndrome (Yu et al, 1996), and RecQL4, the protein mutated in Rothmund-Thomson syndrome (Kitao et al, 1999) and RecQL5 (Shimamoto et al, 2000). Recent biochemical studies have shown that BLM has 3' to 5' DNA-unwinding activity, also possessed by WRN and Sgs1 (Karow et al, 1997;Lu et al, 1996;Suzuki et al, 1997). Among the human RecQ homologues, BLM is most similar to two yeast RecQ-type helicases, Sgs1 and Rqh1 (Stewart et al, 1997;Watt et al, 1996).…”

Section: Introductionmentioning

confidence: 99%