Source:http://linkedlifedata.com/resource/pubmed/id/11443352
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
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| pubmed:dateCreated |
2001-7-9
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| pubmed:databankReference | |
| pubmed:abstractText |
Molecular chaperones mediate the correct folding of nascent or denatured proteins and are found in both the organelles and cytoplasm of eukaryotic cells. Cryptomonad algae are unusual in possessing an extra cytoplasmic compartment (the periplastid space), the result of having engulfed and retained a photosynthetic eukaryote. Within the periplastid space is a diminutive nucleus (the nucleomorph) that encodes mostly genes for its own expression as well as a few needed by the plastid. Two plastid-encoded chaperones (GroEL and DnaK) and a nucleomorph-encoded chaperone (Cpn60) have been reported from the cryptomonad, Guillardia theta. Here we analyse G. theta nucleomorph genes for members of the cytosolic HSP70 and HSP90 families of molecular chaperones, a heat shock transcription factor (HSF), and all eight subunits of the group II chaperonin, CCT. These are presumably all active in the periplastid space, assisting in the maturation of polypeptides required by the cell; we propose a central role for them also in the structure and assembly of a putative relict mitotic apparatus. Curiously, none of the genes for co-chaperones of HSP70, HSP90, or CCT have been detected in the nucleomorph genome; they are either not needed or are encoded in the host nuclear genome and targeted back into the periplastid space. Endoplasmic reticulum (ER) homologs of HSP70 and HSP90 are also not present. Striking differences in the degree of conservation of the various nucleomorph-encoded molecular chaperones were observed. While the G. theta HSP70 and HSP90 homologs are well conserved, each of the eight CCT subunits (alpha, beta, gamma, delta, epsilon, eta, theta, and zeta) is remarkably divergent. Such differences are likely evidence for reduced/different functional constraints on the various molecular chaperones functioning in the periplastid space.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
|
| pubmed:issn |
0022-2844
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
52
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
490-501
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:11443352-Amino Acid Motifs,
pubmed-meshheading:11443352-Amino Acid Sequence,
pubmed-meshheading:11443352-Base Sequence,
pubmed-meshheading:11443352-Cell Nucleus,
pubmed-meshheading:11443352-Cloning, Molecular,
pubmed-meshheading:11443352-Cytosol,
pubmed-meshheading:11443352-Databases, Factual,
pubmed-meshheading:11443352-Endoplasmic Reticulum,
pubmed-meshheading:11443352-Eukaryota,
pubmed-meshheading:11443352-Expressed Sequence Tags,
pubmed-meshheading:11443352-HSP70 Heat-Shock Proteins,
pubmed-meshheading:11443352-HSP90 Heat-Shock Proteins,
pubmed-meshheading:11443352-Mitosis,
pubmed-meshheading:11443352-Models, Genetic,
pubmed-meshheading:11443352-Molecular Chaperones,
pubmed-meshheading:11443352-Molecular Sequence Data,
pubmed-meshheading:11443352-Multigene Family,
pubmed-meshheading:11443352-Phylogeny,
pubmed-meshheading:11443352-Protein Conformation,
pubmed-meshheading:11443352-Saccharomyces cerevisiae,
pubmed-meshheading:11443352-Sequence Analysis, DNA,
pubmed-meshheading:11443352-Sequence Homology, Amino Acid
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| pubmed:year |
2001
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| pubmed:articleTitle |
Molecular chaperones encoded by a reduced nucleus: the cryptomonad nucleomorph.
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| pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia, B3H 4H7, Canada.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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