Abstract:
:The small heat shock protein SsHSP14.1 from the hyper-thermophilic archeaon, Sulfolobus solfataricus (S. solfataricus) was able to protect proteins from thermal aggregation and prevent enzymes from heat induced inactivation. According to the 3D (dimensional) structural model of SsHSP14.1 developed by us before, the region L5-7 (β5-β7, 68-82 residues) plays an important role for the oligomerization of SsHSP14.1 and its chaperone function. Here, to validate the findings, an in-depth investigation was conducted of both the wild type SsHSP14.1 and its deletion mutant DEL75-79. With E. coli proteins and bromelain as substrate, the deletion mutant DEL75-79 can protect them from thermo-aggregating as effective as the wild protein. Interestingly, unlike the wild protein, DEL75-79 was unable to prevent bromelain and EcoRI from thermo-inactivating. Results of size exclusion HPLC showed that the oligomerization state was changed in mutant protein. This was in accordance with the changed structure and lower hydrophobicity of DEL75-79. These outcomes proved that the L5-7 loop did play a role for the oligomerizing SsHSP14.1, and that the residues 75-79 were indispensable for its function of prevent enzymes from thermo-inactivating.
journal_name
Protein Pept Lettjournal_title
Protein and peptide lettersauthors
Wen ZZ,Wang YH,Yang B,Xie MQ,Chou KCdoi
10.2174/092986611794578369subject
Has Abstractpub_date
2011-03-01 00:00:00pages
275-81issue
3eissn
0929-8665issn
1875-5305pii
BSP/ PPL/ E pub/0221journal_volume
18pub_type
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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