The essential mitotic target of calmodulin is the 110-kilodalton component of the spindle pole body in Saccharomyces cerevisiae.

A Mutational Analysis Identifies Three Functional Regions of the Spindle Pole Component Spc110p inSaccharomyces cerevisiae

“…Two additional classes of carboxy-terminal mutations were isolated: 1) mutations that result in truncation of Spc110p; and 2) mutations in the calmodulinbinding region (amino acids 897-917) (Table 3B). We did not explore the role of truncations of Spc110p in conferring temperature sensitivity because previously we demonstrated that conversion of the codon for amino acid 856 to a nonsense codon was not lethal and did not confer a temperature-sensitive phenotype (Geiser et al, 1993). Only one missense mutation was isolated in the region between amino acids 856 and 898, thus further suggesting that this region is unimportant for Spc110p function.…”

“…The gapped pHS33 plasmid contains homology to both ends of the mutagenized PCR product. Mutagenized PCR product (1 g) was cotransformed with 100 ng of gel-purified gapped NcoI-BamHI pHS33 plasmid and 20 l of sheared salmon sperm DNA (20 mg/ml) into the plasmid shuffle indicator strain HSY2-1C (pHS26) (Geiser et al, 1993). Homologous recombination between the gapped pHS33 plasmid ends and the mutagenized DNA ends repairs the gapped plasmid, introducing mutations into SPC110.…”

“…The calmodulin-Spc110p interaction is required for proper chromosome segregation (Geiser et al, 1993;Kilmartin and Goh, 1996;Stirling et al, 1996;Sundberg et al, 1996). Characterization of the carboxy-terminal temperature-sensitive allele spc110 -220, which has a mutation in the calmodulin-binding site, revealed that calmodulin binding to Spc110p is required for the proper assembly of spindle pole components.…”

“…Spc110p is hypothesized to connect the ␥-tubulin complex in the inner plaque to the central plaque (Kilmartin and Goh, 1996). The carboxy terminus of Spc110p, which contains a calmodulin-binding site (amino acids 897-917) (Geiser et al, 1993;Stirling et al, 1994;Spang et al, 1996b), is located at the central plaque of the SPB . The amino terminus of Spc110p is located at the inner plaque (Spang et al, 1996b).…”

The Centrosome and Its Duplication Cycle

“…These g-tubulin docking motifs are highly conserved from human pericentrin and kendrin through Drosophila centrosomin (CNN) to fission yeast Mto1 and Pcp1 (Flory et al 2002;Zhang and Megraw 2007;Fong et al 2008;Samejima et al 2008;Lin et al 2014). Spc29 links Spc110 to the hexagonal crystalline lattice of Spc42 that comprises the central plaque in a coupling that relies on association of Spc110 with calmodulin (Geiser et al 1993;Stirling et al 1994;Donaldson and Kilmartin 1996;Spang et al 1996;Bullit et al 1997;Sundberg and Davis 1997;Elliott et al 1999). On the cytoplasmic side of the central plaque, Spc42 anchors the Cnm67 linker protein that recruits Nud1 to the base of the outer plaque (Adams and Kilmartin 1999;Elliott et al 1999;Schaerer et al 2001).…”