Multi-subunit assembly of the Pyrococcus furiosus small heat shock protein is essential for cellular protection at high temperature.

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TitleMulti-subunit assembly of the Pyrococcus furiosus small heat shock protein is essential for cellular protection at high temperature.
Publication TypeJournal Article
Year of Publication2003
AuthorsLaksanalamai, P, Jiemjit, A, Bu, Z, Maeder, DL, Robb, FT
JournalExtremophiles
Volume7
Issue1
Pagination79-83
Date Published2003 Feb
ISSN1431-0651
Keywordsalpha-Crystallins, Archaeal Proteins, Base Sequence, Dimerization, DNA, Archaeal, Heat-Shock Proteins, Hot Temperature, Models, Molecular, Protein Structure, Quaternary, Protein Subunits, Pyrococcus furiosus, Recombinant Proteins, Sequence Deletion
Abstract

The hyperthermophilic archaeon, Pyrococcus furiosus, expresses a small, alpha-crystallin-like protein in response to exposure to extreme temperatures, above 103 degrees C. The P. furiosus small heat shock protein (Pfu-sHSP) forms large oligomeric complexes. Based on the available crystal structures of the Methanocaldococcus jannaschii and wheat sHSPs, the protruding carboxy terminal domain is probably involved in subunit interactions. We constructed Pfu-sHSP mutants to analyze chaperone function and to study multi-subunit assembly. The results confirmed that the carboxy terminus of Pfu-sHSP is involved in inter-dimer interactions, whereas the amino terminal deletion mutant still exhibited the wild-type assembly characteristics. The ability to form oligomeric complexes via the carboxy terminal domain was shown to be necessary for thermotolerance of Escherichia coli overexpressing Pfu-sHSP. The amino terminal domain was not required for inter-species thermotolerance.

DOI10.1007/s00792-002-0298-z
Alternate JournalExtremophiles
PubMed ID12579383