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강세병

Kang, Sebyung
Protein Nanobio Lab.
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dc.citation.number 1 -
dc.citation.startPage 68 -
dc.citation.title MICROBIAL CELL FACTORIES -
dc.citation.volume 13 -
dc.contributor.author Raghunathan, Govindan -
dc.contributor.author Munussami, Ganapathiraman -
dc.contributor.author Moon, Hyojin -
dc.contributor.author Paik, Hyun-jong -
dc.contributor.author An, Seong Soo A -
dc.contributor.author Kim, Yong-Sung -
dc.contributor.author Kang, Sebyung -
dc.contributor.author Lee, Sun-Gu -
dc.date.accessioned 2023-12-22T02:40:50Z -
dc.date.available 2023-12-22T02:40:50Z -
dc.date.created 2014-06-25 -
dc.date.issued 2014-05 -
dc.description.abstract Background: Inclusion bodies (IBs) were generally considered to be inactive protein deposits and did not hold any attractive values in biotechnological applications. Recently, some IBs of recombinant proteins were confirmed to show their functional properties such as enzyme activities, fluorescence, etc. Such biologically active IBs are not commonly formed, but they have great potentials in the fields of biocatalysis, material science and nanotechnology. Results: In this study, we characterized the IBs of DL4, a deletion variant of green fluorescent protein which forms active intracellular aggregates. The DL4 proteins expressed in Escherichia coli were exclusively deposited to IBs, and the IBs were estimated to be mostly composed of active proteins. The spectral properties and quantum yield of the DL4 variant in the active IBs were almost same with those of its native protein. Refolding and stability studies revealed that the deletion mutation in DL4 didn't affect the folding efficiency of the protein, but destabilized its structure. Analyses specific for amyloid-like structures informed that the inner architecture of DL4 IBs might be amorphous rather than well-organized. The diameter of fluorescent DL4 IBs could be decreased up to 100-200 nm by reducing the expression time of the protein in vivo. Conclusions: To our knowledge, DL4 is the first GFP variant that folds correctly but aggregates exclusively in vivo without any self-aggregating/assembling tags. The fluorescent DL4 IBs have potentials to be used as fluorescent biomaterials. This study also suggests that biologically active IBs can be achieved through engineering a target protein itself. -
dc.identifier.bibliographicCitation MICROBIAL CELL FACTORIES, v.13, no.1, pp.68 -
dc.identifier.doi 10.1186/1475-2859-13-68 -
dc.identifier.issn 1475-2859 -
dc.identifier.scopusid 2-s2.0-84901985879 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/5083 -
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84901985879 -
dc.identifier.wosid 000336994700001 -
dc.language 영어 -
dc.publisher BIOMED CENTRAL LTD -
dc.title A variant of green fluorescent protein exclusively deposited to active intracellular inclusion bodies -
dc.type Article -
dc.description.isOpenAccess TRUE -
dc.relation.journalWebOfScienceCategory Biotechnology & Applied Microbiology -
dc.relation.journalResearchArea Biotechnology & Applied Microbiology -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -

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