Abstract
PELPK1, a novel Arabidopsis thaliana gene was earlier annotated to encode a protein of sub-family, PELPK under hydroxyproline-rich glycoprotein (HRGP) super-family of proteins. Previous bioinformatics and computational analyses predicted PELPK1 to contain an amino-terminal signal peptide destined towards the secretory pathway. In the present study, transgenic plants were developed harboring a translational fusion construct comprising of PELPK1 coding sequence (PELPK1-CDS) and green fluorescent protein (GFP) reporter to determine the localization of PELPK1 in Arabidopsis plants. By employing the techniques of confocal laser scanning microscopy, immunolabeling of GFP with quantum dot (Q-dot), and transmission electron microscopy (TEM), it is shown that the translational fusion product is predominantly deposited to the cell wall. These results are in agreement with the earlier bioinformatics prediction that the PELPK1 is transported via the secretory pathway.
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