Figure 6: Stability of arginylated PRPS depends on mRNA structure and the N-terminally encoded Lys. | Nature Communications

Figure 6: Stability of arginylated PRPS depends on mRNA structure and the N-terminally encoded Lys.

From: Arginylation regulates purine nucleotide biosynthesis by enhancing the activity of phosphoribosyl pyrophosphate synthase

Figure 6

(a) Comparison of the amino-acid sequences of the N-terminal regions of PRPS1 and PRSP2. Boxes show the locations of important positions (5 and 18) for lysine residues that only exist in PRPS1 but not in PRPS2. (b) The free-energy profiles of mRNA folding along the nucleotide sequences of PRPS1 and PRPS2 transcripts in the vicinity of start codons predicted using window lengths of 30 nt. The positions of the start codon AUG, as well as codon positions 5 and 18 are indicated. (c) Left: steady-state levels of R-PRPS1 expressed as a native sequence (WT) or with point mutations at ubiquitination-eligible Lys residues to Arg (K5R and K18R). Error bars represent s.e.m. (n=3). Right: steady-state levels of native R-PRPS2 (WT) or with point mutations at positions 5 and 18 to ubiquitination-eligible Lys (V15K and R18K). Error bars represent s.e.m. (n=3).

Back to article page