ArticleMolecular and cellular biochemistry2001
Cloning and characterization of the cDNA coding for the catalytic alpha subunit of CK2 from tobacco.
Article in Molecular and cellular biochemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 13 citations in OpenAlex.
- High-Throughput Sequencing Reveals Novel microRNAs Involved in the Continuous Flowering Trait of Longan (International journal of molecular sciences · 2022Article
- Phosphorylation of TGB1 by protein kinase CK2 promotes barley stripe mosaic virus movement in monocots and dicots.Journal of experimental botany · 2015Article
- Phosphorylation of the potyvirus capsid protein by protein kinase CK2 and its relevance for virus infection.The Plant cell · 2003Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously reported the participation of the protein kinase CK2 in the mechanism by which salicylic acid activates transcription of genes, such as those coding for glutathion S-transferases, in tobacco. With the purpose of further studying the participation of CK2 in this signal transduction pathway, we isolated and sequenced the cDNA from the NtCK2A gene, coding for the catalytic alpha subunit of CK2 from tobacco. The NtCK2A cDNA was isolated by screening of a tobacco cDNA library with a heterologous probe from Arabidopsis thaliana, followed by 3' RACE to obtain the 3' region. Sequence analysis of the NtCK2A cDNA showed a high level of identity between this CK2alpha protein sequence and the corresponding sequences of other plant species such as Arabidopsis and maize (92-95% identity), or those of animal species such as human and Xenopus laevis (75% identity). The expression of the NtCK2A gene in different tissues from tobacco plants was analyzed by Northern blot. High levels of expression of this gene were observed in proliferating tissues such as shoot and root apical meristems. A recombinant CK2alpha protein was obtained after expression of the NtCK2A cDNA in Escherichia coli. The ability of this recombinant CK2alpha subunit to phosphorylate casein was inhibited by heparin and stimulated by the CK2beta subunit from Xenopus laevis.
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11827163W1506034533What OpenQuestion holds
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