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GFD1 mRNA transport factor Following transcription, mRNA is processed, packaged into messenger ribonucleoprotein (mRNP) particles, and transported through nuclear pores (NPCs) to the cytoplasm. Gfd1 is one of several factors that, although not essential for mRNA export, enhances the efficiency of the process, either by facilitating integration of different steps in the gene expression pathway or by increasing the rate of key steps. Gfd1 localizes to the cytoplasm and nuclear rim. It interacts with a number of components of the mRNA export machinery in yeast. Most notably, Gfd1 interacts with the Dbp5-activating protein, Gle1, the cytoplasmic nucleoporin Nup42/Rip1, the putative RNA helicase, Dbp5, and a protein implicated in mRNA export, Zds1. Gfd1 forms a complex with Nab2 both in vitro and in vivo in which Gfd1 binds to the N-terminal domain of Nab2. The crystal structure, together with complementary NMR data, indicated that residues 126-150 of Gfd1 form a single alpha-helix that binds primarily to helix 2 of Nab2-N. Gfd1 functions to co-ordinate Dbp5 and Gle1 to facilitate the removal of Nab2 from mRNPs at the cytoplasmic face of nuclear pores. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",