Steven J. Brill

TL;DR: It is proposed that the MMS4/SLX3, SLX5/8, and SLX1/4 gene pairs encode heterodimeric complexes and speculate that these complexes are required to resolve recombination intermediates that arise in response to DNA damage, during meiosis, and in the absence of SGS1/TOP3.

TL;DR: Mus81-Mms4 and Rad1-Rad10 are homologous structure-specific endonucleases that cleave 3′ branches from distinct substrates and are required for replication fork stability and nucleotide excision repair, respectively, in the yeast Saccharomyces cerevisiae, and show inverse substrate specificity.

TL;DR: Biochemical studies demonstrate that recombinant Rmi1 is a structure-specific DNA binding protein with a preference for cruciform structures and it is proposed that the DNA binding specificity of RMI1 plays a role in targeting Sgs1-Top3 to appropriate substrates.

TL;DR: It is demonstrated that the highly conserved N-terminal domain of S. cerevisiae Asf1 (Asf1N) is the core region that mediates all tested functions of the full-length protein, and this core region adopts a compact immunoglobulin-fold structure with distinct surface characteristics, including a Hir protein binding region required for gene silencing.

TL;DR: It is concluded that the amino terminus of Sgs1 has an essential role in SGS1 function, distinct from that of the DNA helicase, with which it genetically interacts.