Source:http://linkedlifedata.com/resource/pubmed/id/10993152
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
2001-2-5
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pubmed:databankReference | |
pubmed:abstractText |
The nucleotide sequence of hiC12, isolated as a cDNA clone of hardening-induced Chlorella (hiC) genes, was identified. The clone encodes a late embryogenesis abundant (LEA) protein having six repeats of a 11-mer amino acid motif, although in a slightly imperfect form. To overexpress the hiC61) and hiC12 genes, their coding regions were PCR amplified and subcloned into a pGEX-1lambdaT vector. The HIC6 and HIC12 proteins were expressed as GST fusion proteins in E. coli, then purified. The two HIC proteins were found to be effective in protecting a freeze-labile enzyme, LDH, against freeze-inactivation. On a molar concentration basis, they were about 3.1 x 10(6) times more effective in protecting LDH than sucrose and as effective as BSA. Cryoprotection tests with five kinds of chain-shortened polypeptides, synthesized based on the 11-mer amino acid motif of the HIC6 protein showed that the cryoprotective activity decreased with a decrease in the repeating units of the 11-mer motif. In fact, cryoprotective activities of three kinds of single 11-mer amino acids were very low even at high concentrations. All the results suggested that the sufficiently repeated 11-mer motif is required for the cryoprotective activities of Chlorella LEA proteins.
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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 |
Aug
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pubmed:issn |
0916-8451
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1656-63
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10993152-Amino Acid Sequence,
pubmed-meshheading:10993152-Base Sequence,
pubmed-meshheading:10993152-Chlorella,
pubmed-meshheading:10993152-Cryoprotective Agents,
pubmed-meshheading:10993152-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10993152-L-Lactate Dehydrogenase,
pubmed-meshheading:10993152-Molecular Sequence Data,
pubmed-meshheading:10993152-Plant Proteins,
pubmed-meshheading:10993152-Protein Conformation,
pubmed-meshheading:10993152-Sequence Alignment,
pubmed-meshheading:10993152-Structure-Activity Relationship
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pubmed:year |
2000
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pubmed:articleTitle |
Cryoprotective activities of group 3 late embryogenesis abundant proteins from Chlorella vulgaris C-27.
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pubmed:affiliation |
Department of Bioscience and Biotechnology, Graduate School, Kyushu University, Fukuoka, Japan. honjoh@agr.kyushu-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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