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  • 1
    ISSN: 1573-5028
    Keywords: cloning ; nucleotide sequence ; light regulation ; organ-specific expression ; oxygen evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have identified and isolated cDNA clones of the 33 kDa protein of the oxygen-evolving complex (OEE1) from Lycopersicon esculentum (tomato) and Arabidopsis thaliana and determined their nucleotide sequences. The cDNA clones and antibodies prepared against OEE1 were used as probes to examine the expression of the oee1 gene with respect to regulation by light, organ specificity, and ripening stage of tomato fruit. The steady-state mRNA level is regulated by light, being present in light-grown plants and absent in etiolated seedlings. The oee1 transcripts that accumulate during growth in the light were reduced to non-detectable or low levels by a 3-day dark treatment. The oee1 gene also exhibits differential expression in various organs of the tomato plant. Steady-state mRNA level was highest in immature leaves and absent in roots while the protein was most abundant in mature leaves and absent in roots. During tomato fruit ripening oee1 mRNA decreases to a low level in the pericarp while the protein level decreases below detection. The expression of oee1 appears to be under the control of a complex mechanism regulating both the amount of RNA and its translation.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5028
    Keywords: Arabidopsis ; cloning ; ribonucleoprotein ; RNA-binding ; RNP ; sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated a 1148 bp long cDNA clone encoding an RNA-binding protein in Arabidopsis. Several partial cDNA clones were isolated by screening an Arabidopsis λgt11 expression library for the binding of DNA. One of these clones was used as a probe to isolate a full-length clone. The 329 amino acid protein, termed RNP-T, contains in its carboxy terminus two adjacent RNP-80 motifs, a previously described 80 amino acid long conserved putative RNA-binding domain. Each RNP-80 motif includes both consensus short sequences, RNP1 and RNP2, which are separated by 33 amino acids. We have identified an acidic domain of 54 amino acids, which is located amino-terminal to the RNP-80 motifs. Seven tandem repeats of a hexamer are present within this domain. This acidic domain has a potential α-helix conformation. We propose that the acidic patch might play a role in protein-protein interaction.
    Type of Medium: Electronic Resource
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