heparin/arabidopsis

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

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

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 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

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

Arabidopsis Long Hypocotyl in Far-Red Light 1 (HFR1), a bHLH transcription factor, plays a critical role in promoting seedling photomorphogenesis and in balancing the shade-avoidance response under canopy shade conditions. Previous studies have established that HFR1 protein is degraded in darkness

To study the phosphorylation of one of the G-box binding factors from Arabidopsis (GBF1), we have obtained large amounts of this protein by expression in Escherichia coli. Bacterial GBF1 was shown to be phosphorylated very efficiently by nuclear extracts from broccoli. The phosphorylation activity

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