File Download

There are no files associated with this item.

  • Find it @ UNIST can give you direct access to the published full text of this article. (UNISTARs only)
Related Researcher

박종화

Bhak, Jong
KOrean GenomIcs Center
Read More

Views & Downloads

Detailed Information

Cited time in webofscience Cited time in scopus
Metadata Downloads

Full metadata record

DC Field Value Language
dc.citation.endPage 308 -
dc.citation.number 3 -
dc.citation.startPage 300 -
dc.citation.title JOURNAL OF MICROBIOLOGY -
dc.citation.volume 46 -
dc.contributor.author Shin, Bong-Jeong -
dc.contributor.author Oh, Jeehyun -
dc.contributor.author Kang, Sungsoo -
dc.contributor.author Chung, Young-Ho -
dc.contributor.author Park, Young Mok -
dc.contributor.author Kim, Young Hwan -
dc.contributor.author Kim, Seungil -
dc.contributor.author Bhak, Jong Hwa -
dc.contributor.author Choi, Jong-Soon -
dc.date.accessioned 2023-12-22T08:39:09Z -
dc.date.available 2023-12-22T08:39:09Z -
dc.date.created 2015-07-31 -
dc.date.issued 2008-06 -
dc.description.abstract The unicellular cyanobacterium Synechocystis sp. PCC 6803 glides toward a light source through the interplay of positive phototaxis genes and proteins. In genetic analysis, the complete disruption of the hybrid sensory kinase sll0043 produced negative phototaxis. Furthermore, Sll0043 was found to be a hub protein by in silico prediction of protein-protein interaction, in which Sll0043 was predominantly linked to seven two-component proteins with high confidence. To understand the regulation and networking of positive phototaxis proteins, the proteomic profile of the sll0043 mutant was compared to that of wild-type. In the sll0043 mutant, 18 spots corresponding to 15 unique proteins were altered by 1.3 to 59 fold; the spots were identified by 2-DE/MALDI-MS analysis. Down-regulated proteins in the sll0043 null-mutant included chaperonins, superoxide dismutase, and phycocyanin beta-subunit. In contrast, nine proteins involved in photosynthesis, translation, regulatory function, and other functions were up-regulated. In particular, a twitching motility protein (PilT1) was induced over 2-fold in sll0043 mutant. Moreover, semi-quantitative and quantitative RT-PCR analysis revealed that pilin (pilA1), pili motor (pilT1), and pili switch gene (pilT2) were significantly increased in sll0043 mutant. These results suggest that the hybrid kinase Sll0043 regulates positive phototaxis by suppressing the expression of pili biosynthesis and regulatory genes and through the interplay with positive phototaxis/motility two-component proteins -
dc.identifier.bibliographicCitation JOURNAL OF MICROBIOLOGY, v.46, no.3, pp.300 - 308 -
dc.identifier.doi 10.1007/s12275-007-0212-6 -
dc.identifier.issn 1225-8873 -
dc.identifier.scopusid 2-s2.0-46749096854 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/13235 -
dc.identifier.url http://link.springer.com/article/10.1007%2Fs12275-007-0212-6 -
dc.identifier.wosid 000257240800010 -
dc.language 영어 -
dc.publisher MICROBIOLOGICAL SOCIETY KOREA -
dc.title.alternative Cyanobacterial hybrid kinase SLL0043 regulates phototaxis by suppressing pilin and twitching motility protein. -
dc.title Cyanobacterial hybrid kinase Sll0043 regulates phototaxis by suppressing pilin and twitching motility protein -
dc.type Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor cyanobacteria -
dc.subject.keywordAuthor two-component system -
dc.subject.keywordAuthor positive phototaxis -
dc.subject.keywordAuthor 2-DE/MALD1-MS -
dc.subject.keywordAuthor RT-PCR -
dc.subject.keywordAuthor protein-protein interaction network -
dc.subject.keywordPlus SYNECHOCYSTIS SP PCC-6803 -
dc.subject.keywordPlus SIGNAL-TRANSDUCTION -
dc.subject.keywordPlus UNICELLULAR CYANOBACTERIUM -
dc.subject.keywordPlus PILUS BIOGENESIS -
dc.subject.keywordPlus STRAIN PCC6803 -
dc.subject.keywordPlus PCC 6803 -
dc.subject.keywordPlus LIGHT -
dc.subject.keywordPlus GENES -
dc.subject.keywordPlus STRESS -
dc.subject.keywordPlus EXPRESSION -

qrcode

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