Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/60316
DC FieldValueLanguage
dc.contributor.authorLin, C.H.en_US
dc.contributor.author翁淑芬zh_TW
dc.contributor.authorLee, C.N.en_US
dc.contributor.authorLin, J.W.en_US
dc.contributor.authorTsai, W.J.en_US
dc.contributor.authorWang, S.W.en_US
dc.contributor.authorWeng, S.F.en_US
dc.contributor.authorTseng, Y.H.en_US
dc.date2010zh_TW
dc.date.accessioned2014-06-09T05:56:13Z-
dc.date.available2014-06-09T05:56:13Z-
dc.identifier.issn0175-7598zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/60316-
dc.description.abstracthspA 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.en_US
dc.language.isoen_USzh_TW
dc.relationApplied Microbiology and Biotechnologyen_US
dc.relation.ispartofseriesApplied Microbiology and Biotechnology, Volume 88, Issue 3, Page(s) 699-709.en_US
dc.relation.urihttp://dx.doi.org/10.1007/s00253-010-2776-zen_US
dc.subjectSmall heat shock proteinen_US
dc.subjectXanthomonas campestrisen_US
dc.subjectHspAen_US
dc.subjectphage phi-lfen_US
dc.subjectalpha-crystallinen_US
dc.subjectmethanococcus-jannaschiien_US
dc.subjectin-vitroen_US
dc.subjectchaperoneen_US
dc.subjectgeneen_US
dc.subjectdisaggregationen_US
dc.subjectexpressionen_US
dc.subjectrangeen_US
dc.subjectvivoen_US
dc.titleCharacterization of Xanthomonas campestris pv. campestris heat shock protein A (HspA), which possesses an intrinsic ability to reactivate inactivated proteinsen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1007/s00253-010-2776-zzh_TW
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextno fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en_US-
item.openairetypeJournal Article-
Appears in Collections:分子生物學研究所
Show simple item record
 

Google ScholarTM

Check

Altmetric

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.