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The surprising complexity of peroxisome biogenesis

dc.contributor.authorOlsen, Laura J.en_US
dc.date.accessioned2006-09-08T21:27:10Z
dc.date.available2006-09-08T21:27:10Z
dc.date.issued1998-09en_US
dc.identifier.citationOlsen, Laura J.; (1998). "The surprising complexity of peroxisome biogenesis." Plant Molecular Biology 38 (1-2): 163-189. <http://hdl.handle.net/2027.42/43447>en_US
dc.identifier.issn0167-4412en_US
dc.identifier.issn1573-5028en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/43447
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9738966&dopt=citationen_US
dc.description.abstractPeroxisomes are small organelles with a single boundary membrane. All of their matrix proteins are nuclear-encoded, synthesized on free ribosomes in the cytosol, and post-translationally transported into the organelle. This may sound familiar, but in fact, peroxisome biogenesis is proving to be surprisingly unique. First, there are several classes of plant peroxisomes, each specialized for a different metabolic function and sequestering specific matrix enzymes. Second, although the mechanisms of peroxisomal protein import are conserved between the classes, multiple pathways of protein targeting and translocation have been defined. At least two different types of targeting signals direct proteins to the peroxisome matrix. The most common peroxisomal targeting signal is a tripeptide limited to the carboxyl terminus of the protein. Some peroxisomal proteins possess an amino-terminal signal which may be cleaved after import. Each targeting signal interacts with a different cytosolic receptor; other cytosolic factors or chaperones may also form a complex with the peroxisomal protein before it docks on the membrane. Peroxisomes have the unusual capacity to import proteins that are fully folded or assembled into oligomers. Although at least 20 proteins (mostly peroxins) are required for peroxisome biogenesis, the role of only a few of these have been determined. Future efforts will be directed towards an understanding of how these proteins interact and contribute to the complex process of protein import into peroxisomes.en_US
dc.format.extent210132 bytes
dc.format.extent3115 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherKluwer Academic Publishers; Springer Science+Business Mediaen_US
dc.subject.otherLife Sciencesen_US
dc.subject.otherPlant Sciencesen_US
dc.subject.otherPlant Pathologyen_US
dc.subject.otherGlyoxysomesen_US
dc.subject.otherPeroxisomesen_US
dc.subject.otherPeroxinsen_US
dc.subject.otherProtein Importen_US
dc.subject.otherProtein Targetingen_US
dc.subject.otherBiochemistry, Generalen_US
dc.titleThe surprising complexity of peroxisome biogenesisen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelGeneticsen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biology, University of Michigan, Ann Arbor, MI, 48109-1048, USA (e-mailen_US
dc.contributor.affiliationumcampusAnn Arboren_US
dc.identifier.pmid9738966en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/43447/1/11103_2004_Article_168305.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1023/A:1006092830670en_US
dc.identifier.sourcePlant Molecular Biologyen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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