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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1997-5-13
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pubmed:databankReference |
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pubmed:abstractText |
A phosphoenolpyruvate carboxylase (PEPCase) cDNA was isolated from Aloe arborescens, a monocot CAM plant. Northern analysis of the PEPCase transcript indicated that it is specifically expressed in green leaves, strongly suggesting its involvement in CAM photosynthesis. No diurnal change in expression level was evident. Western blot analysis also showed no alteration of the amount of the PEPCase protein. These results suggest that circadian rhythm in PEPCase activity may be regulated post-translationally. The representative cDNA clone contained an ORF encoding 964 amino acid residues. Deduced amino acid sequence of the aloe PEPCase is highly conserved as compared with other PEPCases. The phosphorylation site which may be modified by PEPC-kinase was conserved. An evolutional map with known PEPCases suggested that CAM-type PEPCases were located between C4 and housekeeping PEPCases.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0032-0781
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
881-8
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pubmed:dateRevised |
2001-11-28
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pubmed:meshHeading |
pubmed-meshheading:8888625-Aloe,
pubmed-meshheading:8888625-Amino Acid Sequence,
pubmed-meshheading:8888625-Base Sequence,
pubmed-meshheading:8888625-DNA, Complementary,
pubmed-meshheading:8888625-DNA, Plant,
pubmed-meshheading:8888625-Gene Expression,
pubmed-meshheading:8888625-Molecular Sequence Data,
pubmed-meshheading:8888625-Phosphoenolpyruvate Carboxylase,
pubmed-meshheading:8888625-Phylogeny,
pubmed-meshheading:8888625-Plant Proteins,
pubmed-meshheading:8888625-Plants, Medicinal
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pubmed:year |
1996
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pubmed:articleTitle |
Isolation of a cDNA for a phosphoenolpyruvate carboxylase from a monocot CAM-plant, Aloe arborescens: structure and its gene expression.
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pubmed:affiliation |
Life Science Institute, Mitsui Toatsu Chemicals, Inc., Mobara, Japan.
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pubmed:publicationType |
Journal Article
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