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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

SLX4  -  Slx4p

Saccharomyces cerevisiae S288c

Synonyms: L3140, Structure-specific endonuclease subunit SLX4, YLR135W
 
 
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High impact information on SLX4

  • The Slx1-Slx4 nuclease is active on branched DNA substrates, particularly simple-Y, 5'-flap, or replication fork structures [1].
  • Deletion of SLX4 conferred many of the same DNA-repair defects observed in rtt107delta, including DNA damage sensitivity, prolonged DNA damage checkpoint activation, and increased spontaneous DNA damage [2].
  • Slx4 regulates DNA damage checkpoint-dependent phosphorylation of the BRCT domain protein Rtt107/Esc4 [2].
  • These results suggest that Mre11 (with Sae2) and Slx4 represent two new structure-specific endonucleases that protect cells from trapped topoisomerase by removing topoisomerase-DNA adducts [3].
  • Here, we report the isolation and characterization of temperature-sensitive (ts) SGS1 alleles in cells lacking SLX4 [4].
 

Biological context of SLX4

  • The Saccharomyces cerevisiae SLX4 gene is required for cell viability in the absence of Sgs1, the only yeast RecQ helicase [5].
  • Slx1-Slx4 was reported to preferentially cleave replication fork-like structures in vitro, and cells lacking SLX4 are hypersensitive to DNA alkylation damage [5].
  • At the non-permissive temperature (37 degrees C) sgs1-ts slx4 cells progress through S-phase and arrest growth as large-budded cells with at least a 2C DNA content [4].
  • These results suggest that Sgs1 and Slx4 are not required for bulk DNA synthesis but play redundant roles in maintaining rDNA structure during DNA replication [4].
  • These results reveal Slx4 as a new target of the Mec1/Tel1 kinases, with a crucial role in DNA repair that is not restricted to the processing of stalled replisomes [5].
 

Physical interactions of SLX4

  • A two-hybrid screen showed that the N-terminal BRCT motifs of Rtt107/Esc4 bound to Slx4, a protein previously shown to be involved in DNA repair and required for viability in a strain lacking the DNA helicase Sgs1 [6].
 

Other interactions of SLX4

  • CONCLUSION: Rtt107/Esc4 binds to the silencing protein Sir3 and the DNA repair protein Slx4 via different BRCT motifs, thus providing a bridge linking silent chromatin to DNA repair enzymes [6].

References

  1. Slx1-Slx4 is a second structure-specific endonuclease functionally redundant with Sgs1-Top3. Fricke, W.M., Brill, S.J. Genes Dev. (2003) [Pubmed]
  2. Slx4 regulates DNA damage checkpoint-dependent phosphorylation of the BRCT domain protein Rtt107/Esc4. Roberts, T.M., Kobor, M.S., Bastin-Shanower, S.A., Ii, M., Horte, S.A., Gin, J.W., Emili, A., Rine, J., Brill, S.J., Brown, G.W. Mol. Biol. Cell (2006) [Pubmed]
  3. Multiple endonucleases function to repair covalent topoisomerase I complexes in Saccharomyces cerevisiae. Deng, C., Brown, J.A., You, D., Brown, J.M. Genetics (2005) [Pubmed]
  4. Role of SGS1 and SLX4 in maintaining rDNA structure in Saccharomyces cerevisiae. Kaliraman, V., Brill, S.J. Curr. Genet. (2002) [Pubmed]
  5. Slx4 becomes phosphorylated after DNA damage in a Mec1/Tel1-dependent manner and is required for repair of DNA alkylation damage. Flott, S., Rouse, J. Biochem. J. (2005) [Pubmed]
  6. Rtt107/Esc4 binds silent chromatin and DNA repair proteins using different BRCT motifs. Zappulla, D.C., Maharaj, A.S., Connelly, J.J., Jockusch, R.A., Sternglanz, R. BMC Mol. Biol. (2006) [Pubmed]
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