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An in silico prediction of interaction models of influenza a virus PA and human C14orf166 protein from yeast-two-hybrid screening data
  • Kadir TURAN,
  • Elif Çağlayan
Marmara Universitesi Eczacilik Fakultesi

Corresponding Author:[email protected]

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Elif Çağlayan
Kartal Kosuyolu Yuksek Ihtisas Egitim ve Arastirma Hastanesi
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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.
18 Aug 2022Submitted to PROTEINS: Structure, Function, and Bioinformatics
18 Aug 2022Submission Checks Completed
18 Aug 2022Assigned to Editor
02 Sep 2022Reviewer(s) Assigned
17 Apr 2023Review(s) Completed, Editorial Evaluation Pending
21 Apr 2023Editorial Decision: Revise Minor
16 May 20231st Revision Received
16 May 2023Submission Checks Completed
16 May 2023Assigned to Editor
16 May 2023Review(s) Completed, Editorial Evaluation Pending
18 May 2023Editorial Decision: Accept