Molecular characterization of Oryza sativa 16.9 kDa heat shock protein

Li Sen Young, Ching Hui Yeh, Yih Ming Chen, Chu Yung Lin

研究成果: 雜誌貢獻期刊論文同行評審

16 引文 斯高帕斯(Scopus)

摘要

A rice class I low-molecular-mass heat shock protein (LMM HSP) Oshsp16.9 was overexpressed in Escherichia coli. Oligomerized complexes of Oshsp16.9 were harvested and electron microscopic observations of purified complexes revealed globular structures of 10-20 nm in diameter (with majority of 15-18 nm) and calculated to comprise approx. 12 monomers per complex. In comparison, complexes from native rice class I LMM HSPs were observed as larger ellipsoid- or globular-like random aggregated hetero-oligomers. To characterize the biochemical functions of the hydrophobic N-terminal region of Oshsp16.9, a truncation in the N-terminal region was constructed and introduced into E. coli. Results showed that the N-terminal truncated Oshsp16.9 mutant was capable of forming complexes similar to the full-length Oshsp16.9; however, the deletion protein failed to confer in vitro protein thermostability under elevated temperatures. Protein assays from in vivo treatments at higher temperatures exhibited that non-specific interactions of E. coli cellular proteins only occurred with full-length Oshsp16.9 complexes but not with the mutant complex. In vitro immunoprecipitation of cellular proteins from E. coli overexpressing full-length Oshsp16.9 showed that interactions between plant LMM HSP and E. coli cellular proteins are temperature-dependent. Taken together, the hydrophobic N-terminal region of rice class I LMM HSP is critical in the ability of the protein to interact/bind with its potential substrates.

原文???core.languages.en_GB???
頁(從 - 到)31-38
頁數8
期刊Biochemical Journal
344
發行號1
DOIs
出版狀態已出版 - 15 11月 1999

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