The human C14orf166 protein, also known as RTRAF, shows positive
modulatory activity on the cellular RNA polymerase II enzyme. This
protein is a component of the tRNA-splicing ligase complex and is
involved in RNA metabolism. It also functions in the nucleo-cytoplasmic
transport of RNA molecules. The C14orf166 protein has been reported to
be associated with some types of cancer. It has been shown that the
C14orf166 protein binds to the influenza A virus RNA polymerase PA
subunit and has a stimulating effect on viral replication. In this
study, candidate interactor proteins for influenza A virus PA protein
were screened with a Y2H assay using HEK293 Matchmaker cDNA. The
C14orf166 protein fragments in different sizes were found to interact
with the PA. The three-dimensional structures of the viral PA and
C14orf166 proteins interacting with the PA were generated using the
I-TASSER algorithm. The interaction models between these proteins were
predicted with the ClusPro protein docking algorithm and analyzed with
PyMol software. The results revealed that the carboxy-terminal end of
the C14orf166 protein is involved in this interaction, and it is highly
possible that it binds to the carboxy-terminal of the PA protein.
Although amino acid residues in the interaction area of the PA protein
with the C14orf166 showed distribution from 450th to 700th position, the
intense interaction region was revealed to be at amino acid positions
610 to 630.