Document Type
Article
Publication Date
5-1-1998
Publication Title
Nucleic Acids Research
Department
Geisel School of Medicine
Abstract
QSR1 is a highly conserved gene which encodes a 60S ribosomal subunit protein that is required for joining of large and small ribosomal subunits. In this report we demonstrate heterologous complementation of a yeast QSR1 deletion strain with both the human and corn homologs and show that the human and corn proteins are assembled into hybrid yeast/human and yeast/corn ribosomes. While the homologous genes complement lethality of the QSR1 deletion, they also result in a diminished growth rate. Analyses of the translation rates of ribosomes containing the human and corn proteins reveal a partial loss of function. Velocity gradient analyses of the hybrid ribosomes after exposure to high concentrations of salt indicate that the decreased activity is due to lability of the hybrid 60S subunits.
DOI
10.1093/nar/26.10.2442
Original Citation
Dick FA, Trumpower BL. Heterologous complementation reveals that mutant alleles of QSR1 render 60S ribosomal subunits unstable and translationally inactive. Nucleic Acids Res. 1998;26(10):2442-2448. doi:10.1093/nar/26.10.2442
Dartmouth Digital Commons Citation
Dick, Frederick A. and Trumpower, Bernard L., "Heterologous Complementation Reveals that Mutant Alleles of QSR1 Render 60S Ribosomal Subunits Unstable and Translationally Inactive" (1998). Dartmouth Scholarship. 3817.
https://digitalcommons.dartmouth.edu/facoa/3817
