Yeast calmodulin

More recently, workers in Japan published the solution structure of yeast (Saccharomyces cerevisiae) apo-calmodulin (PDB ILKJ). Yeast calmodulin is 60% identical in its amino acid sequence with vertebrate CaMs. The ILKJ N-terminal domain with its two helix-loop-helix calcium-binding domains looks quite similar to those of IDMO and ICFD (see Figure 6.23). 

Davis, T. N., Urdea, M. S., Masiarz, F.R. and Thorner, J. (1986) Isolation of the yeast calmodulin gene calmodulin is an essential protein. Cell 47, 423-431. 

Hong, S. P., Momcilovic, M. and Carlson, M., 2005, Function of mammalian LKB1 and Ca2+/calmodulin-dependent protein kinase kinase alpha as Snfl-activating kinases in yeast, J Biol Chem, 280, pp 21804-9. 

Structures of the motor domains of three different kinesin-14 proteins, kinesins with a C-terminal motor domain, have been determined so far (1) the Drosophila nonclaret disjunctional gene product (DmNcd), (2) the yeast kinesin-like nuclear fusion protein (ScKar3), and (3) the kinesin-like calmodulin binding protein from potato (PoKCBP). 

Calmodulin (CaM) is a ubiquitous intracellular protein that mediates more than 100 different biological systems in both calcium-free and -loaded forms. CaM has 148 amino acids and its primary sequence is highly conserved in all cell types. It shares strong sequence and stmcture homology to TnC, which is involved solely in the Calcimn-dependent regulation of skeletal and heart muscle contraction. Yeast (yCaM) is 60% identical in sequence to vertebrate CaMs and contains only three functional sites. Several labs have shown that the prokaryotes have several CaM-like proteins containing two or more authentic EF-hand motifs. ... 

Garrett-Engele R, Moilanen B., and Cyert M.S. 1995. Calcineurin, the Ca /calmodulin-dependent protein phosphatase is essential in yeast mutants with cell integrity defects and in mutants that lack a functional vacuolar H -ATPase. Mol Cell Biol 15 4103-4114. 

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