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About that time, David Engelke's group reported the identification of 9 proteins in the RNase P of the yeast nucleus. All of these proteins are essential for RNase P activity in vivo. These proteins, even if they only occur once for every RNA molecule, add up to more than twice the mass of the RNA, and none of these proteins are recognizably similar to the bacterial protein. Most of these proteins have homologs in other eukaryotes, including humans. The roles of these proteins in RNase P function are still under investigation, but reconstitution of RNase P activity from these proteins and the RNA have not yet been accomplished.

Could Archaea contain RNase P proteins homologous to eukaryotic proteins rather than those of Bacteria?