The surprising complexity of peroxisome biogenesis
dc.contributor.author | Olsen, Laura J. | en_US |
dc.date.accessioned | 2006-09-08T21:27:10Z | |
dc.date.available | 2006-09-08T21:27:10Z | |
dc.date.issued | 1998-09 | en_US |
dc.identifier.citation | Olsen, 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.issn | 0167-4412 | en_US |
dc.identifier.issn | 1573-5028 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/43447 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9738966&dopt=citation | en_US |
dc.description.abstract | Peroxisomes 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.extent | 210132 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers; Springer Science+Business Media | en_US |
dc.subject.other | Life Sciences | en_US |
dc.subject.other | Plant Sciences | en_US |
dc.subject.other | Plant Pathology | en_US |
dc.subject.other | Glyoxysomes | en_US |
dc.subject.other | Peroxisomes | en_US |
dc.subject.other | Peroxins | en_US |
dc.subject.other | Protein Import | en_US |
dc.subject.other | Protein Targeting | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.title | The surprising complexity of peroxisome biogenesis | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Genetics | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biology, University of Michigan, Ann Arbor, MI, 48109-1048, USA (e-mail | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 9738966 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/43447/1/11103_2004_Article_168305.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1023/A:1006092830670 | en_US |
dc.identifier.source | Plant Molecular Biology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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