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• W1484254996 abstract "Human catalase forms a 240‐kDa tetrameric complex and degrades H 2 O 2 in peroxisomes. Human catalase is targeted to peroxisomes by the interaction of its peroxisomal targeting signal type 1 ( PTS1 )‐like KANL sequence with the cytosolic PTS1 receptor Pex5p. We show herein that human catalase tetramers are formed in the cytoplasm and that the expression of a PTS signal on each of the four subunits is not necessary for peroxisomal transport. We previously demonstrated that a Pex5p mutant defective in binding to Pex13p, designated Pex5p(Mut234), imports typical PTS1 ‐type proteins but not catalase. This impaired catalase import is not rescued by replacing its C‐terminal KANL sequence with a typical PTS1 sequence, SKL , indicating that the failure of catalase import in Mut234‐expressing cells is not due to its weak PTS1 . In contrast, several enzymatically inactive and monomeric mutants of catalase are efficiently imported in Mut234‐expressing cells. Moreover, trimeric chloramphenicol acetyltransferase ( CAT ) harboring SKL is not imported in Pex5p(Mut234)‐expressing cells, but CAT‐SKL trimers are transported to peroxisomes in the wild‐type cells. These findings suggest that the Pex5p–Pex13p interaction likely plays a pivotal role in the peroxisomal import of folded and oligomeric proteins." @default.
• W1484254996 created "2016-06-24" @default.
• W1484254996 creator A5024899735 @default.
• W1484254996 creator A5053489078 @default.
• W1484254996 date "2012-07-29" @default.
• W1484254996 modified "2023-10-15" @default.
• W1484254996 title "Pex5p Imports Folded Tetrameric Catalase by Interaction with Pex13p" @default.
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• W1484254996 doi "https://doi.org/10.1111/j.1600-0854.2012.01391.x" @default.
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