Human CHP1 and the C. elegans homolog Chp are CHORD domain-containing proteins that are largely related, and their corresponding genes are evolutionarily conserved among various eukaryotic organisms (1,2). The unique CHORD domain is characterized as 60 amino acids in length, and contains six highly conserved cysteine residues, two histidine residues and a distinct Zn2+-binding domain (3). CHP1 and the other metazoan orthologs have tandem CHORD domains that are located at both the N- and C- termini (1,4). These proteins are implicated in germline development and embryogenesis as mutations affecting the CHORD domain of the nematode protein Chp result in semisterility and embryonic lethality (1,5).