heparin/arabidopsis thaliana

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Heparin stimulates a plasma membrane Ca2+-ATPase of Arabidopsis thaliana.

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We have studied the effect of heparin, a glycosaminoglycan widely used in releasing tags from fusion proteins, on isoform 8 of Arabidopsis thaliana PM Ca(2+)-ATPase (ACA8) expressed in Saccharomyces cerevisiae strain K616. Heparin stimulates hydrolytic activity of ACA8 with an estimated K(0.5) value

Cloning and characterization of two cDNAs encoding casein kinase II catalytic subunits in Arabidopsis thaliana.

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Two cDNA clones, ATCKA1 and ATCKA2, encoding casein kinase II (CKII) catalytic subunits, were cloned from Arabidopsis thaliana and their nucleotide sequences were determined. Both cDNAs contain 999 bp open reading frames and are 94% identical on the amino acid sequence level. The deduced amino acid

A negative regulatory factor for the dark repression of Arabidopsis thaliana cab1 gene.

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A protein factor and its binding site involved in light-responsive gene expression of Arabidopsis thaliana cab1 were investigated. Mobility shift assays were performed to identify a nuclear protein factor and its binding sites on the cab1 promoter. For the binding assay, the Arabidopsis cab1

The peptide microarray "ChloroPhos1.0" identifies new phosphorylation targets of plastid casein kinase II (pCKII) in Arabidopsis thaliana.

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We report the development of a peptide microarray based on previously determined phosphorylation sites in chloroplast proteins. Altogether, 905 peptides were spotted as 15mers in nine replicates onto glass slides. We used the microarray for in vitro phosphorylation experiments and specifically

Cloning and characterization of the cDNA coding for the catalytic alpha subunit of CK2 from tobacco.

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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

tRNA-assisted overproduction of eukaryotic ribosomal proteins.

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Structural studies of eukaryotic ribosomes are complicated by the tendency of their constituent proteins to be expressed at very low levels in Escherichia coli. We find that this is mainly due to their exceptionally high content of AGA/AGG arginine codons, which are poorly utilized by the bacterial

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