RGD Reference Report - The effect of mutating arginine-469 on the substrate binding and refolding activities of 70-kDa heat shock cognate protein. - Rat Genome Database

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The effect of mutating arginine-469 on the substrate binding and refolding activities of 70-kDa heat shock cognate protein.

Authors: Chang, TC  Hsiao, CD  Wu, SJ  Wang, C 
Citation: Chang TC, etal., Arch Biochem Biophys. 2001 Feb 1;386(1):30-6.
RGD ID: 10059391
Pubmed: PMID:11360998   (View Abstract at PubMed)
DOI: DOI:10.1006/abbi.2000.2176   (Journal Full-text)

On the basis of the X-ray structure of DnaK, we obtained an energy-minimized model for the C-terminal domain of rat 70-kDa heat shock cognate protein (hsc70). The model suggests that Arg-469 may play an important role in maintaining the substrate-bound conformation of hsc70. To verify this hypothesis, we substituted cysteine for Arg-469 and generated the hsc70(R469C) mutant. Compared to the wild-type hsc70, the mutant was more accessible to cleavage by endopeptidase Lys-C, implying that the overall structure of hsc70(R469C) is relatively loose. Moreover, hsc70(R469C) did not form tightly associated complexes with S-carboxymethyl-alpha-lactalbumin, an unfolded protein. The amount of heptapeptide FYQLALT bound to hsc70(R469C) was also decreased as determined by gel filtration. Thus, the affinity of hsc70(R469C) for polypeptide substrates is reduced. In the presence of DnaJ, the capability of hsc70(R469C) to refold the denatured luciferase was decreased by 50%. Therefore, for hsc70, reduction in affinity for substrates may affect its DnaJ-dependent refolding activity.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Hspa8Ratpositive regulation of protein refolding  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Hspa8  (heat shock protein family A (Hsp70) member 8)


Additional Information