结合EGFR 3'UTR的蛋白质复合物的分离与鉴定

In recent years, the function of Untranslated region(UTR) serves as one of the hotspots of biological research.There are some regulatory elements in the UTR of mRNA sequences, such as the stem loop structure. A number of proteins or protein complex may interact with these regulatory elements which may have an impact on mRNA transcription, processing, nuclear export and subcellular localization, translation and post-translational modifications consequently. Epidermal growth factor receptor(EGFR) is the key factor in singal transduction. Therefore, the function of EGFR UTR in cells is particularly important. In our study, the method of affinity pull down was used to isolate and identifie proteins or protein complex interacting with EGFR 3'UTR from whole cell lysate of HeLa. And then the MALDI-TOF-TOF mass spectrometry was used to analyse these proteins or protein complexes in order to clarify the potential function of EGFR 3'UTR in mRNA transport, mRNA stability, subcellular localization or translation. In our study, seven proteins which may interacted with EGFR 3'UTR have been identified using mass spectrometry. Among these proteins, hnRNP Q, hnRNP I, hnRNP A3, hnRNP A1 and hnRNP A2/B1 belong to heterogeneous nuclear ribonucleoprotein family. Other proteins including interleukin enhancer binding factor 3(ILF3) and hyaluronic acid receptor-mediated migration(RHAMM). These proteins we have identified in this study were mostly RNA binding proteins (RBP), which could be involved in maintaining stability, subcellular localization and protein translation of mRNA. The findings in our study will provide some reference valuable to further investigate the regulatory mechanism of EGFR 3'UTR.