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Chemical Compound Review

Ser-lys-leu     (2S)-2-[[(2S)-6-amino-2- [[(2S)-2-amino-3...

Synonyms: Skl tripeptide, AC1L2YSO, 130488-05-0, Seryl-lysyl-leucine, N-(N2-L-Seryl-L-lysyl)-L-leucine, ...
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High impact information on Skl tripeptide

  • The aim of our studies was to analyze cell lines from six different complementation groups in a systematic manner for the presence of peroxisome ghosts, the ability to import Ser-Lys-Leu-containing proteins into peroxisome ghosts and for the presence of cytosolic factors required for peroxisomal protein import [1].
  • To examine the structural requirements for organellar localization, the Ser-Lys-Leu carboxyl-terminal tripeptide, a common motif for localization of peroxisomal proteins, was removed by mutagenesis of the MDH3 gene [2].
  • The MDH3 sequence was found to contain a carboxyl-terminal SKL tripeptide, characteristic of many peroxisomal enzymes, and immunochemical analysis was used to confirm organellar localization of the MDH3 isozyme [3].
  • Carboxyl-terminal sequences Ser-Lys-Leu (SKL) and Leu-Gln-Ser-Lys-Leu (LQSKL) of acyl-CoA oxidase (AOX) directed to peroxisomes the fused proteins with import-incompetent forms of AOX and catalase that had been truncated, implying that the SKL tripeptide functions as a targeting signal [4].
  • They also suggest that the non-consensus PTS1 of human AGT might interact with HsPex5p very differently compared with the consensus PTS1, Ser-Lys-Leu [5].

Biological context of Skl tripeptide

  • The open reading frame contains an N-terminal mitochondrial targeting sequence and the C-terminal part of the enzyme ends with a peroxisomal (Ser-Lys-Leu) targeting motif [6].
  • The deduced amino acid sequence displays a terminal tripeptide Ser-Lys-Ile which is highly homologous to the PTS (Ser-Lys-Leu) found in other peroxisomal enzymes [7].
  • The mutant cells exhibited a temperature-sensitive (TS) phenotype on the peroxisomal localizations of the recombinant GFP and urate oxidase appending a genuine peroxisome targeting signal 1 (PTS1), a tripeptide of Ser-Lys-Leu (SKL) at the C-terminus, but did not on that of catalase harboring a divergent PTS1, Lys-Ala-Asn-Leu (KANL) sequence [8].

Anatomical context of Skl tripeptide


Gene context of Skl tripeptide

  • Although the nucleotide and deduced amino acid sequences of these cDNAs are almost identical, the deduced HPR1 protein contains Ser-Lys-Leu at its carboxy-terminal end, which is known as a microbody-targeting signal, while the deduced HPR2 protein does not [10].
  • Rat liver catalase is sorted to peroxisomes by its C-terminal tripeptide Ala-Asn-Leu, not by the internal Ser-Lys-Leu motif [11].
  • A synthetic peptide composed of the C-terminal 10 amino acid residues of acyl-CoA oxidase (the C-terminal tripeptide is Ser-Lys-Leu) inhibited the import of urate oxidase, whereas other peptides, in which the C-terminal Ser-Lys-Leu (SKL) sequence was deleted or mutated, were not effective [12].

Analytical, diagnostic and therapeutic context of Skl tripeptide

  • This report describes the microinjection of two proteins, (i) luciferase and (ii) albumin conjugated to a peptide ending in the sequence Ser-Lys-Leu, into mammalian cells grown in tissue culture [13].


  1. Presence of cytoplasmic factors functional in peroxisomal protein import implicates organelle-associated defects in several human peroxisomal disorders. Wendland, M., Subramani, S. J. Clin. Invest. (1993) [Pubmed]
  2. Expression and function of a mislocalized form of peroxisomal malate dehydrogenase (MDH3) in yeast. McAlister-Henn, L., Steffan, J.S., Minard, K.I., Anderson, S.L. J. Biol. Chem. (1995) [Pubmed]
  3. Isolation and characterization of the yeast gene encoding the MDH3 isozyme of malate dehydrogenase. Steffan, J.S., McAlister-Henn, L. J. Biol. Chem. (1992) [Pubmed]
  4. Carboxyl-terminal consensus Ser-Lys-Leu-related tripeptide of peroxisomal proteins functions in vitro as a minimal peroxisome-targeting signal. Miura, S., Kasuya-Arai, I., Mori, H., Miyazawa, S., Osumi, T., Hashimoto, T., Fujiki, Y. J. Biol. Chem. (1992) [Pubmed]
  5. The peroxisomal targeting sequence type 1 receptor, Pex5p, and the peroxisomal import efficiency of alanine:glyoxylate aminotransferase. Knott, T.G., Birdsey, G.M., Sinclair, K.E., Gallagher, I.M., Purdue, P.E., Danpure, C.J. Biochem. J. (2000) [Pubmed]
  6. Cloning and expression of rat pancreatic beta-cell malonyl-CoA decarboxylase. Voilley, N., Roduit, R., Vicaretti, R., Bonny, C., Waeber, G., Dyck, J.R., Lopaschuk, G.D., Prentki, M. Biochem. J. (1999) [Pubmed]
  7. An impaired peroxisomal targeting sequence leading to an unusual bicompartmental distribution of cytosolic epoxide hydrolase. Arand, M., Knehr, M., Thomas, H., Zeller, H.D., Oesch, F. FEBS Lett. (1991) [Pubmed]
  8. Temperature-sensitive phenotype of Chinese hamster ovary cells defective in PEX5 gene. Ito, R., Huang, Y., Yao, C., Shimozawa, N., Suzuki, Y., Kondo, N., Imanaka, T., Usuda, N., Ito, M. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  9. Characterization of Aspergillus nidulans peroxisomes by immunoelectron microscopy. Valenciano, S., De Lucas, J.R., Van der Klei, I., Veenhuis, M., Laborda, F. Arch. Microbiol. (1998) [Pubmed]
  10. Pumpkin hydroxypyruvate reductases with and without a putative C-terminal signal for targeting to microbodies may be produced by alternative splicing. Hayashi, M., Tsugeki, R., Kondo, M., Mori, H., Nishimura, M. Plant Mol. Biol. (1996) [Pubmed]
  11. Rat liver catalase is sorted to peroxisomes by its C-terminal tripeptide Ala-Asn-Leu, not by the internal Ser-Lys-Leu motif. Trelease, R.N., Xie, W., Lee, M.S., Mullen, R.T. Eur. J. Cell Biol. (1996) [Pubmed]
  12. Urate oxidase is imported into peroxisomes recognizing the C-terminal SKL motif of proteins. Miura, S., Oda, T., Funai, T., Ito, M., Okada, Y., Ichiyama, A. Eur. J. Biochem. (1994) [Pubmed]
  13. Transport of microinjected proteins into peroxisomes of mammalian cells: inability of Zellweger cell lines to import proteins with the SKL tripeptide peroxisomal targeting signal. Walton, P.A., Gould, S.J., Feramisco, J.R., Subramani, S. Mol. Cell. Biol. (1992) [Pubmed]
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