The Many Interfaces of Mre11 James E Haber  Cell  Volume 95, Issue 5, Pages 583-586 (November 1998) DOI: 10.1016/S0092-8674(00)81626-8

Figure 1 Seven Roles for Mre11/Rad50/Xrs2 Proteins in Saccharomyces In conjunction with many different sets of proteins, the Mre11 complex performs a surprisingly large range of functions, ranging from helping the Spo11 topoisomerase to create double-strand breaks during meiosis, to the maintenance of telomeres, to various types of repair and processing of double strand breaks in both meiosis and mitosis. These proteins also play a role in the checkpoint responses of cells to the presence of a chromosome break. The human NBS homolog of Xrs2p is defective in Nijmegen breakage syndrome. Many other roles in mammalian cells have been inferred but the absence of viable mutants of Mre11p or Rad50p has prevented a direct assessment of their functions. Cell 1998 95, 583-586DOI: (10.1016/S0092-8674(00)81626-8)

Figure 2 Important Subdomains of the Mre11 Protein Identified in Saccharomyces The amino-terminal part of Mre11p is evolutionarily well conserved, especially in several subregions (red). The C-terminal part of the protein is also conserved, and contains two DNA-binding domains (Usui et al. 1998). Several representative base pair substitution mutations that eliminate nuclease activity (marked by X) are shown and discussed in the text, including the mre11S mutation that alters two sites in the 692–amino acid protein. Three terminal truncation mutations (indicated by a black line) that specifically abolish the ability of meiotic cells to produce double-strand breaks are shown. mre11-T10 was created by a transposon insertion, whereas the other two mutants were produced by introducing nonsense mutations. Cell 1998 95, 583-586DOI: (10.1016/S0092-8674(00)81626-8)