High impact information on GFD1

• In a screen for high-copy suppressors of the rat8-2 allele of DBP5, we identified YMR255w, now called GFD1 [1].
• Here we reported that Dbp5p and Gfd1p interact with Zds1p, a protein previously identified as a multicopy suppressor in several yeast genetic screens [2].
• Here we report that Nab2, Gfd1, and Gle1 associate in a complex [3].
• Nuclear export of the yeast mRNA-binding protein Nab2 is linked to a direct interaction with Gfd1 and to Gle1 function [3].
• To investigate glycerol biosynthesis in T. atroviride, the genes encoding glycerol dehydrogenase (gld1) and glycerol-3-phosphate dehydrogenase (gfd1) were cloned and characterized [4].

Anatomical context of GFD1

• We proposed that Zds1p associates with the complex formed by Dbp5p, Gfd1p, and nucleoporins at the cytosolic fibrils of the nuclear pore complex and is required for optimal mRNA export [2].

Physical interactions of GFD1

• This N-terminal Nab2 domain is distinct from its RNA binding domains suggesting Nab2 could bind Gfd1 and RNA simultaneously [3].

Other interactions of GFD1

• Sequencing indicated that a 2.1-kb subclone encompasses the very end (last 11 amino acids) of the PET111 gene, the COX7 gene and a new gene (YMR255W) of unknown function that potentially codes for a polypeptide of 188 amino acids (about 21.5 kDa) without significant homology to any known protein [5].
• A Nab2-Gfd1 complex was also identified by coimmunoprecipitation from yeast lysates [3].

References