In humans, transport of histones H3/H4 from the cytoplasm to the nucleus occurs in a stepwise fashion and is mediated by protein factors including HSP90, NASP, Asf1 and Importin4. Cells can adopt two different pathways to assemble chromatin, namely replication dependent and replication independent pathways which are mediated respectively by “Chromatin Assembly Factor 1 (CAF1)” and “Histone Regulator A (HIRA)” protein complexes. Despite their identification, the mechanistic details of H3/H4 transport and subsequent deposition onto DNA remains unclear. To address this, we have performed proteomic characterization of Asf1, NASP, CAF1 and Hat1 in Tetrahymena using affinity purification combined with mass spectrometry approach. Tetrahymena is an excellent model system to study chromatin related processes providing that it features nuclear dualism in the form of a transcriptionally active macronucleus and a silent micronucleus. Our results indicate that NASP physically interacts with Asf1 and HSP90 and thus likely functions in H3/H4 transport suggesting an evolutionarily conserved nature of this pathway. We also show that the three protein CAF1 complex (Cac1, Cac2, Cac3) interacts with H3/H4 as well as with Casein Kinase 2 (CK2), an evolutionary conserved SER/THR protein kinase. Our MS data also indicates that Hat1 co-purifies with H4 and a putative Hat2 protein. Interestingly, we found that Hat2 subunit of HAT complex is also shared by CAF1 complex as its Cac3 subunit. We have named this protein SSCH1 (Shared Subunit of CAF-1 and Hat1). This suggest that SSCH1 exists in two separate pools of protein complexes and is capable of carrying functions that are divided between two separate proteins in higher eukaryotes such as humans.