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  Identification and analysis of the plant peroxisomal targeting signal 1 receptor NtPEX5

Kragler, F., Lametschwandtner, G., Christmann, J., Hartig, A., & Harada, J. J. (1998). Identification and analysis of the plant peroxisomal targeting signal 1 receptor NtPEX5. In Proceedings of the National Academy of Sciences of the United States of America (pp. 13336-13341).

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-35EE-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-35EF-1
Genre: Conference Paper

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Kragler, F.1, Author              
Lametschwandtner, G.1, Author
Christmann, J.1, Author
Hartig, A.1, Author
Harada, J. J.1, Author
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1External Organizations, ou_persistent22              

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Free keywords: Amino Acid Sequence Animals Binding Sites Cloning, Molecular Escherichia coli/genetics Humans Mammals Molecular Sequence Data Peptide Fragments/chemistry/metabolism *Plants, Toxic Receptors, Cytoplasmic and Nuclear/chemistry/*genetics/metabolism Recombinant Proteins/chemistry/metabolism Saccharomyces cerevisiae/genetics Sequence Alignment Sequence Homology, Amino Acid Tobacco/*genetics/metabolism
 Abstract: Protein translocation into peroxisomes takes place via recognition of a peroxisomal targeting signal present at either the extreme C termini (PTS1) or N termini (PTS2) of matrix proteins. In mammals and yeast, the peroxisomal targeting signal receptor, Pex5p, recognizes the PTS1 consisting of -SKL or variants thereof. Although many plant peroxisomal matrix proteins are transported through the PTS1 pathway, little is known about the PTS1 receptor or any other peroxisome assembly protein from plants. We cloned tobacco (Nicotiana tabacum) cDNAs encoding Pex5p (NtPEX5) based on the protein's interaction with a PTS1-containing protein in the yeast two-hybrid system. Nucleotide sequence analysis revealed that the tobacco Pex5p contains seven tetratricopeptide repeats and that NtPEX5 shares greater sequence similarity with its homolog from humans than from yeast. Expression of NtPEX5 fusion proteins, consisting of the N-terminal part of yeast Pex5p and the C-terminal region of NtPEX5, in a Saccharomyces cerevisiae pex5 mutant restored protein translocation into peroxisomes. These experiments confirmed the identity of the tobacco protein as a PTS1 receptor and indicated that components of the peroxisomal translocation apparatus are conserved functionally. Two-hybrid assays showed that NtPEX5 interacts with a wide range of PTS1 variants that also interact with the human Pex5p. Interestingly, the C-terminal residues of some of these peptides deviated from the established plant PTS1 consensus sequence. We conclude that there are significant sequence and functional similarities between the plant and human Pex5ps.

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Language(s): eng - English
 Dates: 1998
 Publication Status: Published in print
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Title: Proceedings of the National Academy of Sciences of the United States of America
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Proceedings
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Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 13336 - 13341 Identifier: -