The purpose of this study was to determine whether the plant type 1 peroxisomal targeting signal (PTS1) utilizes @entity535 residues that do not strictly adhere to the @entity563 - @entity376 - @entity368 (SKL) motif (small-basic-hydrophobic residues). Selected residues were appended to the C terminus of @entity2755 acetyltransferase (CAT) and were tested for their ability to target CAT fusion proteins to glyoxysomes in @entity286 ( @entity286 .) cv Bright Yellow 2 suspension-cultured cells. CAT was redirected from the cytosol into glyoxysomes by a wide range of residues, i.e. A/C/G/S/T-H/K/ L/N/R-I/L/M/Y. Although L and N at the -2 position (-SLL, -ANL) do not conform to the SKL motif, both functioned, but in a temporally less-efficient manner. Other SKL divergent residues, however, did not target CAT to glyoxysomes, i.e. F or P at the -3 position (-FKL, -PKL), S or T at the -2 position (-SSI, STL), or D at the -1 position (-SKD). The targeting inefficiency of CAT-ANL could be ameliorated when K was included at the -4 position (-KANL). In summary, the plant PTS1 mostly conforms to the SKL motif. For those PTS1s that possess nonconforming residue(s), other residues upstream of the PTS1 appear to function as accessory sequences that enhance the temporal efficiency of peroxisomal targeting.

Diverse XXXX residues function within the type 1 peroxisomal targeting signal. Implications for the role of accessory residues upstream of the type 1 peroxisomal targeting signal.

@entity286 :: ('4097', 'Species') :: ['Nicotiana tabacum L', 'tobacco'] @entity368 :: ('CHEBI:25017', 'Chemical') :: ['leucine'] @entity535 :: ('CHEBI:33704', 'Chemical') :: ['amino acid'] @entity376 :: ('CHEBI:25094', 'Chemical') :: ['lysine'] @entity563 :: ('CHEBI:17822', 'Chemical') :: ['serine'] @entity2755 :: ('MESH:D002701', 'Chemical') :: ['chloramphenicol']
@entity535 :: (CHEBI:33704,Chemical) :: ['amino acid']
