A conserved and essential basic region mediates tRNA binding to the Elp1 subunit of the Saccharomyces cerevisiae Elongator complex.
Bottom Line: Since these modifications are required for the tRNAs to function efficiently, a translation defect caused by hypomodified tRNAs may therefore underlie the variety of phenotypes associated with Elongator dysfunction.The Elp1 carboxy-terminal domain contains a highly conserved arginine/lysine-rich region that resembles a nuclear localization sequence (NLS).Thus the conserved basic region in Elp1 may be essential for tRNA wobble uridine modification by acting as tRNA binding motif.
Affiliation: Centre for Gene Regulation & Expression, College of Life Sciences, MSI/WTB Complex, University of Dundee, Dundee, DD1 5EH, Scotland, UK.Show MeSH
Related in: MedlinePlus
Mentions: In agreement with earlier work (Fichtner et al., 2003), we found that the Elp1 C-terminal domain (amino acids 1181–1349) was capable of driving nuclear import of GFP and that this was dependent specifically on the basic region. Thus GFP tagged with the wild-type Elp1 C-terminus was concentrated exclusively in the cell nucleus (Fig. 2), while the elp1–KR9A, elp1–KR5A and elp1–KR4A mutants all showed diffuse localization of GFP throughout the cell that was comparable to that of GFP alone, suggesting that when the basic region is mutated the C-terminus can no longer influence GFP localization. The basic region in the Elp1 carboxy-terminal domain therefore has the potential to drive nuclear import.
Affiliation: Centre for Gene Regulation & Expression, College of Life Sciences, MSI/WTB Complex, University of Dundee, Dundee, DD1 5EH, Scotland, UK.