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PMID:12715159
| Citation |
Pleckaityte, M, Mistiniene, E, Michailoviene, V and Zvirblis, G (2003) Identification and characterization of a Hsp70 (DnaK) chaperone system from Meiothermus ruber. Mol. Genet. Genomics 269:109-15 |
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| Abstract |
We have cloned the genes encoding the chaperones of Meiothermus ruber, Hsp70 (Mru.Hsp70), Hsp40 (Mru.Hsp40) and Hsp22 (Mru.Hsp22). The genes hsp70, hsp22 and hsp40 of M. ruber are organized into an operon. The amino acid sequences of the three M. ruber chaperones show strong similarity with the heat shock proteins of Thermus thermophilus. Both Mru.Hsp40 and its homolog from T. thermophilus lack a cysteine-rich region. However, recombinant Mru.Hsp70 and Mru.Hsp40 associate in an ATP-dependent manner, and assemble into a complex in the absence of other proteins, unlike their counterparts from T. thermophilus, which require DafA for assembly. The analysis revealed that Mru.Hsp70 and Mru.Hsp40 assemble as monomers into the complex, although their homologs from T. thermophilus enter the complex as trimers. The Mru.Hsp70 and Mru.Hsp40 complex increases the spontaneous rate of refolding of denatured mitochondrial malate dehydrogenase by tenfold. |
| Links |
PubMed Online version:10.1007/s00438-003-0818-2 |
| Keywords |
Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA, Bacterial/chemistry; DNA, Bacterial/genetics; Gene Expression; Genes, Bacterial/genetics; HSP70 Heat-Shock Proteins/chemistry; HSP70 Heat-Shock Proteins/genetics; HSP70 Heat-Shock Proteins/metabolism; Molecular Sequence Data; Operon; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Species Specificity; Thermus/chemistry; Thermus/classification; Thermus/genetics; Thermus thermophilus/chemistry; Thermus thermophilus/genetics |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0042026: protein refolding |
ECO:0000314: |
P |
Figure 3: Refolding activity of Hsp70 increased in response to denatured mitochondrial malate dehydrogenase. |
complete | ||||
See also
References
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