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https://hdl.handle.net/10216/25360
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DC Field | Value | Language |
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dc.creator | costa-rodrigues, j | |
dc.creator | carvalho, af | |
dc.creator | gouveia, am | |
dc.creator | fransen, m | |
dc.creator | sa-miranda, c | |
dc.creator | azevedo, je | |
dc.date.accessioned | 2022-09-08T09:04:38Z | - |
dc.date.available | 2022-09-08T09:04:38Z | - |
dc.date.issued | 2004 | |
dc.identifier.issn | 0021-9258 | |
dc.identifier.other | sigarra:78136 | |
dc.identifier.uri | https://hdl.handle.net/10216/25360 | - |
dc.description.abstract | Most newly synthesized peroxisomal matrix proteins are transported to the organelle by Pex5p, a remarkable multidomain protein involved in an intricate network of transient protein-protein interactions. Presently, our knowledge regarding the structure/function of amino acid residues 118 to the very last residue of mammalian Pex5p is quite vast. Indeed, the cargo-protein receptor domain as well as the binding sites for several peroxins have all been mapped to this region of Pex5p. In contrast, structural/functional data regarding the first 117 amino acid residues of Pex5p are still scarce. Here we show that a truncated Pex5p lacking the first 110 amino acid residues (DeltaN110-Pex5p) displays exactly the peroxisomal import properties of the full-length peroxin implying that this N-terminal domain is involved neither in cargo-protein binding nor in the docking/translocation step of the Pex5p-cargo protein complex at the peroxisomal membrane. However, the ATP-dependent export step of DeltaN110-Pex5p from the peroxisomal membrane is completely blocked, a phenomenon that was also observed for a Pex5p version lacking just the first 17 amino acid residues but not for a truncated protein comprising amino acid residues 1-324 of Pex5p. By exploring the unique properties of DeltaN110-Pex5p, the effect of temperature on the import/export kinetics of Pex5p was characterized. Our data indicate that the export step of Pex5p from the peroxisomal compartment ( in contrast with its insertion into the organelle membrane) is highly dependent on the temperature. | |
dc.language.iso | eng | |
dc.rights | openAccess | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc/4.0/ | |
dc.title | The N terminus of the peroxisomal cycling receptor, Pex5p, is required for redirecting the peroxisome-associated peroxin back to the cytosol | |
dc.type | Artigo em Revista Científica Internacional | |
dc.contributor.uporto | Faculdade de Ciências da Nutrição e Alimentação | |
dc.contributor.uporto | Instituto de Ciências Biomédicas Abel Salazar | |
dc.identifier.doi | 10.1074/jbc.m406399200 | |
dc.identifier.authenticus | P-000-7RQ | |
Appears in Collections: | FCNAUP - Artigo em Revista Científica Internacional ICBAS - Artigo em Revista Científica Internacional |
This item is licensed under a Creative Commons License