DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jung, HJ | - |
dc.contributor.author | Hwang, DS | - |
dc.contributor.author | De Wei, Q | - |
dc.contributor.author | Cha, HJ | - |
dc.contributor.author | 황동수 | - |
dc.date.accessioned | 2016-04-01T02:45:04Z | - |
dc.date.available | 2016-04-01T02:45:04Z | - |
dc.date.issued | 2008-02 | - |
dc.identifier.citation | BIOTECHNOLOGY PROGRESS | - |
dc.identifier.citation | v.24 | - |
dc.identifier.citation | no.1 | - |
dc.identifier.citation | pp.17-22 | - |
dc.identifier.issn | 8756-7938 | - |
dc.identifier.other | 2008-OAK-0000021797 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/25699 | - |
dc.description.abstract | The effective delivery of exogenous genes into eukaryotic cells is important for fundamental and biotechnological research. Protein-based gene delivery including histone proteins has recently emerged as a powerful technique for non-viral DNA transfer. Histories are DNA-binding proteins that function in DNA packaging and protection. In particular, histone H1 is largely responsible for the stabilization of higher-order chromatin structures. Several studies have examined the use of full-length histone H1-mediated gene transfer, and a few studies have investigated the use of C-terminal histone H1 fragments as gene-transfer materials. Previously, we cloned a novel histone H1 cDNA from the goldfish Carassius auratus and found that a recombinant histone H1 C-terminal short peptide (H1C) of 61 amino acids has comparable DNA binding and protection functions as full-length histone H1. In the present work, we successfully expressed and purified soluble recombinant H1 C in an Escherichia coli expression system using a hexahistidine tag fusion strategy and providing tRNAs for rare codons. We confirmed its DNA-binding ability and found that this H1C peptide had similar or higher transfection efficiency in mammalian cells (human 293T and mouse NIH/3T3) than the widely used agent lipofectamine. Therefore, we suggest that this novel goldfish-derived recombinant histone H1 C-terminal short peptide could be used as a peptide-based gene-transfer mediator. | - |
dc.description.statementofresponsibility | X | - |
dc.publisher | Wiley | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | H1-MEDIATED TRANSFECTION | - |
dc.subject | DNA | - |
dc.subject | H1 | - |
dc.subject | EXPRESSION | - |
dc.subject | PROTEIN | - |
dc.subject | BINDING | - |
dc.subject | DOMAIN | - |
dc.subject | IDENTIFICATION | - |
dc.subject | COMPLEXES | - |
dc.title | Carassius auratus-originated recombinant histone H1 c-terminal peptide as Gene delivery material | - |
dc.type | Conference | - |
dc.contributor.college | 해양대학원 | - |
dc.identifier.doi | 10.1021/BP070069B | - |
dc.author.google | Jung, HJ | - |
dc.author.google | Hwang, DS | - |
dc.author.google | De Wei, Q | - |
dc.author.google | Cha, HJ | - |
dc.relation.volume | 24 | - |
dc.relation.issue | 1 | - |
dc.relation.startpage | 17 | - |
dc.relation.lastpage | 22 | - |
dc.contributor.id | 10167197 | - |
dc.publisher.location | US | - |
dc.relation.journal | BIOTECHNOLOGY PROGRESS | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Conference Papers | - |
dc.type.docType | Conference Paper | - |
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