Source:http://linkedlifedata.com/resource/pubmed/id/16830226
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2006-9-14
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pubmed:abstractText |
The DnaE intein of Synechocystis sp. PCC6803 (Ssp DnaE intein) is the first split intein identified in nature. Its N-terminal fragment (Int-n) is attached to the end of the N-terminal half of the DnaE protein (DnaE-n) to form the precursor DnaE-n/Int-n, while the C-terminal fragment (Int-c) precedes the C-terminal half of the DnaE protein (DnaE-c) to form the precursor Int-c/DnaE-c. Int-n and Int-c fragments in the separate precursors catalyze, in concert, a protein trans-splicing process to splice the flanking DnaE-n and DnaE-c into a functional catalytic subunit of DNA polymerase III. They then release themselves from the precursors. Previously, the Ssp DnaE intein has been used to reconstitute a protein trans-splicing mechanism in stably transformed Arabidopsis thaliana, resulting in successful reassembly of an intact and functional GUS from two halves of a split GUS protein. In this report, transient expression using a biolistic particle bombardment approach is described for functional analysis of Ssp DnaE intein. Analyses confirmed that the Ssp DnaE intein could catalyze protein trans-splicing not only in model plants but also in monocot and dicot crops. It also demonstrated that when up to 45 amino acid residues were removed from the C-terminus of the Int-n fragment, the Int-n fragment was still able to function in the protein trans-splicing process.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0962-8819
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
583-93
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pubmed:meshHeading |
pubmed-meshheading:16830226-Amino Acid Sequence,
pubmed-meshheading:16830226-Arabidopsis,
pubmed-meshheading:16830226-Biolistics,
pubmed-meshheading:16830226-DNA Polymerase III,
pubmed-meshheading:16830226-Inteins,
pubmed-meshheading:16830226-Molecular Sequence Data,
pubmed-meshheading:16830226-Recombinant Fusion Proteins,
pubmed-meshheading:16830226-Sequence Deletion,
pubmed-meshheading:16830226-Synechocystis
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pubmed:year |
2006
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pubmed:articleTitle |
Functional analysis of the split Synechocystis DnaE intein in plant tissues by biolistic particle bombardment.
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pubmed:affiliation |
Central Research and Development, E. I. DuPont de Nemours & Co., Experimental Station, Wilmington, DE 19880, USA. jianjun-gene.yang@usa.dupont.com
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pubmed:publicationType |
Journal Article
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