4.5 Article

Coiled-coil motif in LBD16 and LBD18 transcription factors are critical for dimerization and biological function in arabidopsis

期刊

PLANT SIGNALING & BEHAVIOR
卷 13, 期 1, 页码 -

出版社

TAYLOR & FRANCIS INC
DOI: 10.1080/15592324.2017.1411450

关键词

Arabidopsis; lateral organ boundaries domain; LBD16; LBD18; coiled-coil motif; protein-protein interactions; transcriptional regulation; lateral root development

资金

  1. Next-Generation BioGreen 21 Program through the National Research Foundation of Korea - Ministry of Education, Science, and Technology of Korea [PJ01104701]
  2. RDA, Republic of Korea and Mid-career Researcher Program through the National Research Foundation of Korea - Ministry of Education, Science, and Technology of Korea [2016R1A2B4015201]
  3. Basic Research Laboratory through the National Research Foundation of Korea - Ministry of Education, Science, and Technology of Korea [2017R1A4A1015620]

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The LATERAL ORGAN BOUNDARIES (LOB) DOMAIN (LBD) gene family members encode a class of plant-specific transcription factors that play important roles in many different aspects of plant growth and development. The LBD proteins contain a conserved LOB domain harboring a Leu zipper-like coiled-coil motif, which has been predicted to mediate protein-protein interactions among the LBD family members. Dimerization of transcription factors is crucial for the modulation of their DNA-binding affinity, specificity, and diversity, contributing to the transcriptional regulation of distinct cellular and biological responses. Our various molecular and biochemical experiments with genetic approaches on LBD16 and LBD18, which are known to control lateral root development in Arabidopsis, demonstrated that the conserved Leu or Val residues in the coiled-coil motifs of these transcription factors are critical for their dimerization as well as the transcriptional regulation to display their biological functions during lateral root formation. We further showed that beside the coiled-coil motif, the carboxyl-terminal region in LBD18 acts as an additional dimerization domain. These findings provide a molecular framework for the homo- and hetero-dimerization of the LBD family proteins for displaying their distinct and diverse biological functions in plants.

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