NDLI: Subcellular localization and oligomerization of the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 protein.

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Subcellular localization and oligomerization of the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 protein.

Content Provider	Semantic Scholar
Author	Shah, K. Gadella, Theodorus W. J. Erp, Harrie Van Hecht, Vfg Vries, Sacco C. De
Copyright Year	2001
Abstract	The Arabidopsis thaliana somatic embryogenesis receptor kinase 1 (AtSERK1) gene is expressed in developing ovules and early embryos. AtSERK1 is also transiently expressed during somatic embryogenesis. The predicted AtSERK1 protein contains an extracellular domain with a leucine zipper motif followed by five leucine-rich repeats, a proline-rich region, a single transmembrane region and an intracellular kinase domain. The AtSERK1 cDNA was fused to two different variants of green fluorescent protein (GFP), a yellow-emitting GFP (YFP) and a cyan-emitting GFP (CFP), and transiently expressed in both plant protoplasts and insect cells. Using confocal laser scanning microscopy it was determined that the AtSERK1-YFP fusion protein is targeted to plasma membranes in both plant and animal cells. The extracellular leucine-rich repeats, and in particular the N-linked oligosaccharides that are present on them appear to be essential for correct localization of the AtSERK1-YFP protein. The potential for dimerization of the AtSERK1 protein was investigated by measuring the YFP/CFP fluorescence emission ratio using fluorescence spectral imaging microscopy. This ratio will increase due to fluorescence resonance energy transfer if the AtSERK1-CFP and AtSERK1-YFP fusion proteins interact. In 15 % of the cells the YFP/CFP emission ratio for plasma membrane localized AtSERK1 proteins was enhanced. Yeast-protein interaction experiments confirmed the possibility for AtSERK1 homodimerization. Elimination of the extracellular leucine zipper domain reduced the YFP/CFP emission ratio to control levels indicating that without the leucine zipper domain AtSERK1 is monomeric.
File Format	PDF HTM / HTML
DOI	10.1006/jmbi.2001.4706
Alternate Webpage(s)	http://arquivo.ufv.br/DBV/PGFVG/BVE684/htms/pdfs_seminarios/seminario1/n%EF%BF%BDvel_3/express%EF%BF%BDo_genica/lembriogenesisreceptorkinase.pdf
PubMed reference number	11397085
Alternate Webpage(s)	https://doi.org/10.1006/jmbi.2001.4706
Journal	Medline
Volume Number	309
Issue Number	3
Journal	Journal of molecular biology
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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