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Title: Comparative analysis of the conserved functions of Arabidopsis DRL1 and yeast KTI12.
Authors: Jun, S. E.
Cho, K. H.
Hwang, J. Y.
Abdel-Fattah, W.
Hammermeister, A. G.
Schaffrath, Raffael
Bowman, J. L.
Kim, G. T.
First Published: 16-Dec-2014
Publisher: Springer Verlag (Germany) for Korean Society for Molecular and Cellular Biology
Citation: Molecules and Cells, 2015, 38 (3), pp. 243-250
Abstract: Patterning of the polar axis during the early leaf developmental stage is established by cell-to-cell communication between the shoot apical meristem (SAM) and the leaf primordia. In a previous study, we showed that the DRL1 gene, which encodes a homolog of the Elongator-associated protein KTI12 of yeast, acts as a positive regulator of adaxial leaf patterning and shoot meristem activity. To determine the evolutionally conserved functions of DRL1, we performed a comparison of the deduced amino acid sequence of DRL1 and its yeast homolog, KTI12, and found that while overall homology was low, well-conserved domains were presented. DRL1 contained two conserved plant-specific domains. Expression of the DRL1 gene in a yeast KTI12-deficient yeast mutant suppressed the growth retardation phenotype, but did not rescue the caffeine sensitivity, indicating that the role of Arabidopsis Elongator-associated protein is partially conserved with yeast KTI12, but may have changed between yeast and plants in response to caffeine during the course of evolution. In addition, elevated expression of DRL1 gene triggered zymocin sensitivity, while overexpression of KTI12 maintained zymocin resistance, indicating that the function of Arabidopsis DRL1 may not overlap with yeast KTI12 with regards to toxin sensitivity. In this study, expression analysis showed that class-I KNOX genes were downregulated in the shoot apex, and that YAB and KAN were upregulated in leaves of the Arabidopsis drl1-101 mutant. Our results provide insight into the communication network between the SAM and leaf primordia required for the establishment of leaf polarity by mediating histone acetylation or through other mechanisms.
DOI Link: 10.14348/molcells.2015.2297
ISSN: 1016-8478
eISSN: 0219-1032
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2014, Korean Society for Molecular and Cellular Biology. All rights reserved. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit (
Appears in Collections:Published Articles, Dept. of Genetics

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