Targeting signals for protein import into peroxisomes

Targeting sequences of the two major peroxisomal proteins in the methylotrophic yeast Hansenula polymorpha

“…Thirdly, the A-R-F-COOH motif of MOX can similarly be derived from the PTS by a single amino acid exchange, given the fact that the PTS, based on tests of its function in mammalian cells, was shown to be degenerate to a certain extent, as indicated by the consensus sequence of amino acids S-,A-,C-,/K-,H-, R-,/L-COOH (Gould et al 1989). A common feature of all tripetides described so far is also the presence of a hydrophobic residue at the third position and a basic amino acid at the second position (Roggenkamp 1992). In summary, the described targeting signals of H. polymorpha are likely to be novel variants of a C-terminal tripeptide.…”

Peroxisomes and their Assembly in Higher Plants

“…Proteins destined for peroxisomes are nuclear encoded, synthesized on free polyribosomes in the cytoplasm, and posttranslationally transported into the organelle (19, 20, 118,121,151,158,175,176). In recent years, significant advances have been made toward elucidating the mechanisms and the compo nents involved in protein import into peroxisomes.…”

The Difference in Recognition of Terminal Tripeptides as Peroxisomal Targeting Signal 1 between Yeast and Human Is Due to Different Affinities of Their Receptor Pex5p to the Cognate Signal and to Residues Adjacent to It

“…Although PTS1 is conserved throughout evolution (17), its consensus in lower eukaryotes was thought to be broader than in mammals (5,18,19). PTS1 variants such as SKF or SKI direct catalases to peroxisomes of S. cerevisiae and Hansenula polymorpha, respectively (20,21); however, similarly extended luciferases do not reach peroxisomes in monkey kidney cells (22).…”