Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/60316
標題: Characterization of Xanthomonas campestris pv. campestris heat shock protein A (HspA), which possesses an intrinsic ability to reactivate inactivated proteins
作者: Lin, C.H.
翁淑芬
Lee, C.N.
Lin, J.W.
Tsai, W.J.
Wang, S.W.
Weng, S.F.
Tseng, Y.H.
關鍵字: Small heat shock protein;Xanthomonas campestris;HspA;phage phi-lf;alpha-crystallin;methanococcus-jannaschii;in-vitro;chaperone;gene;disaggregation;expression;range;vivo
Project: Applied Microbiology and Biotechnology
期刊/報告no:: Applied Microbiology and Biotechnology, Volume 88, Issue 3, Page(s) 699-709.
摘要: 
hspA encodes a small heat shock protein (sHSP) in Xanthomonas campestris pv. campestris, the causative agent of black rot in cruciferous plants. In this study, two-dimensional gel electrophoresis, promoter activity assays, and Northern hybridization results revealed that HspA expression was induced by heat shock but not by other stresses, although low-level expression was detectable by reverse transcription-polymerase chain reaction (RT-PCR) under normal culture conditions. An hspA mutant exhibited reduced tolerance to heat, especially in the presence of MgSO(4), but no change in pathogenicity. Results of size-exclusion chromatography indicated that purified HspA(his), containing six C-terminal histidine residues, formed two different size classes of oligomeric complexes-410 and 820 kDa. In contrast, HspA(ter), the unmodified protein translated from the original hspA gene, formed only the 820-kDa complex. These results suggest that the C-terminus of HspA is important for oligomerization. Both HspA820(his) and HspA410(his) were able to partially protect luciferase against heat-induced aggregation. Unlike other reported sHSPs that commonly capture denaturing proteins in refoldable states until refolded by adenosine triphosphate-dependent chaperone systems, HspA(his) alone was capable of reactivating heat-inactivated EcoRI. Thus, Xanthomonas campestris pv. campestris HspA has potential application as a protective agent during the storage of proteins.
URI: http://hdl.handle.net/11455/60316
ISSN: 0175-7598
DOI: 10.1007/s00253-010-2776-z
Appears in Collections:分子生物學研究所

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