Casein kinase II interacts with the bZIP domains of several transcription factors

Casein kinase II interacts with the bZIP domains of several transcription factors.

Casein kinase II (CKII) is thought to regulate a broad range of transcription factors, but its mode of action is not well characterized. We previously showed that CKII is co-purified with the ATF family of transcription factors using DNA-affinity latex beads. Here we report a functional and physical interaction between CKII and transcription factors. We demonstrate that CKII binds through its c...

Copurification of casein kinase II with transcription factor ATF/E4TF3.

We have developed a simple method to purify sequence-specific DNA-binding proteins directly from crude cell extracts by using DNA affinity latex beads. The method enabled us to purify not only DNA-binding proteins, but also their associated proteins. Using beads bearing the ATF/E4TF3 site from the adenovirus E4 gene promoter, a protein kinase activity was copurified with the ATF/E4TF3 family. W...

Redox regulation of bZIP transcription factors

From the Department of Plant Physiology and Umeå Plant Science Centre, Umeå University, SE-901 87 Umeå, Sweden Umeå Plant Science Centre, Department of Forest Genetics and Plant Physiology, SLU, SE-901 87 Umeå, Sweden Biochemistry and Physiology of Plants, Faculty of Biology, W5, Bielefeld University, 33501 Bielefeld, Germany Department of Chemistry, Center of Chemical Biology and Computational...

The chaperone ability comparison of norma II-casein and modified d-casein upon interaction with lysozinie

Diminishing protein aggregation by chaperone is very important factor in medicine and industry. In this paper, itis induced the chaperone ability for 0-casein upon modification of its acidic residues by Woodward reagentK(WRK) and examined on lysozyme as a target protein at pH 7.2 and outlined the mechanism for chaperoneability of modified system by UV-Vis and fluorescence spectroscopy and theor...

Running head: bZIP Transcription Factors in Rice