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30. Interactions between Transmembrane Helices within Monomers of the Aquaporin AtPIP2;1 Play a Crucial Role in Tetramer Formation

Author

Yoo, Yun-Joo, primary, Lee, Hyun Kyung, additional, Han, Wonhee, additional, Kim, Dae Heon, additional, Lee, Myoung Hui, additional, Jeon, Jouhyun, additional, Lee, Dong Wook, additional, Lee, Junho, additional, Lee, Yongjik, additional, Lee, Juhun, additional, Kim, Jin Seok, additional, Cho, Yunje, additional, Han, Jin-Kwan, additional, and Hwang, Inhwan, additional

Published
2016
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34. The Vr-PLC3 gene encodes a putative plasma membrane-localized phosphoinositide-specific phospholipase C whose expression is induced by abiotic stress in mung bean (Vigna radiata L.)1<FN ID="FN1"><NO>1</NO>EMBL accession numbers: AY394079 (Vr-PLC1), AY461431 (Vr-PLC2) and AY394078 (Vr-PLC3).</FN>

Author

Kim, Yun Ju, Kim, Jee Eun, Lee, Jae-Hoon, Lee, Myoung Hui, Jung, Ho Won, Bahk, Young Yil, Hwang, Byung Kook, Hwang, Inhwan, and Kim, Woo Taek

Subjects
INOSITE, PHOSPHOLIPASES, GLYCERYL ethers, INOSITOL
Abstract

Phosphoinositide-specific phospholipase C (PI-PLC) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate to generate inositol 1,4,5-trisphosphate and diacylglycerol, both of which act as secondary messengers in animal cells. In this report, we identified in Vigna radiata L. (mung bean) three distinct partial cDNAs (pVr-PLC1, pVr-PLC2, and pVr-PLC3), which encode forms of putative PI-PLC. All three Vr-PLC genes were transcriptionally active and displayed unique patterns of expression. The Vr-PLC1 and Vr-PLC2 transcripts were constitutively expressed to varying degrees in every tissue of mung bean plants examined. In contrast, the Vr-PLC3 mRNA level was very low under normal growth conditions and was rapidly induced in an abscisic acid-independent manner under environmental stress conditions (drought and high salinity). An isolated genomic clone, about 8.2 kb in length, showed that Vr-PLC1 and Vr-PLC3 are in tandem array in the mung bean genome. The predicted primary sequence of Vr-PLC3 (Mr=67.4 kDa) is reminiscent of the δ-isoform of animal enzymes which contain core sequences found in typical PI-PLCs, such as the catalytic domain comprising X and Y motifs, a lipid-binding C2 domain, and the less conserved EF-hand domain. Results of in vivo targeting experiment using a green fluorescent protein (GFP) showed that the GFP-Vr-PLC3 fusion protein was localized primarily to the plasma membrane of the Arabidopsis protoplast. The C2 domain was essential for Vr-PLC3 to be targeted to the plasma membrane. The possible biological functions of stress-responsive Vr-PLC3 in mung bean plants are discussed. [Copyright &y& Elsevier]

Published
2004
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35. The Vr-PLC3 gene encodes a putative plasma membrane-localized phosphoinositide-specific phospholipase C whose expression is induced by abiotic stress in mung bean (Vigna radiata L.)11EMBL accession numbers: AY394079 (Vr-PLC1), AY461431 (Vr-PLC2) and AY394078 (Vr-PLC3)

Author

Kim, Yun Ju, Kim, Jee Eun, Lee, Jae-Hoon, Lee, Myoung Hui, Jung, Ho Won, Bahk, Young Yil, Hwang, Byung Kook, Hwang, Inhwan, and Kim, Woo Taek

Subjects
Phospholipase C, Inositol 1,4,5-trisphosphate, Calcium, Abiotic stress, Vigna radiata, Differential gene expression, Plasma membrane
Abstract

Phosphoinositide-specific phospholipase C (PI-PLC) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate to generate inositol 1,4,5-trisphosphate and diacylglycerol, both of which act as secondary messengers in animal cells. In this report, we identified in Vigna radiata L. (mung bean) three distinct partial cDNAs (pVr-PLC1, pVr-PLC2, and pVr-PLC3), which encode forms of putative PI-PLC. All three Vr-PLC genes were transcriptionally active and displayed unique patterns of expression. The Vr-PLC1 and Vr-PLC2 transcripts were constitutively expressed to varying degrees in every tissue of mung bean plants examined. In contrast, the Vr-PLC3 mRNA level was very low under normal growth conditions and was rapidly induced in an abscisic acid-independent manner under environmental stress conditions (drought and high salinity). An isolated genomic clone, about 8.2 kb in length, showed that Vr-PLC1 and Vr-PLC3 are in tandem array in the mung bean genome. The predicted primary sequence of Vr-PLC3 (Mr=67.4 kDa) is reminiscent of the δ-isoform of animal enzymes which contain core sequences found in typical PI-PLCs, such as the catalytic domain comprising X and Y motifs, a lipid-binding C2 domain, and the less conserved EF-hand domain. Results of in vivo targeting experiment using a green fluorescent protein (GFP) showed that the GFP-Vr-PLC3 fusion protein was localized primarily to the plasma membrane of the Arabidopsis protoplast. The C2 domain was essential for Vr-PLC3 to be targeted to the plasma membrane. The possible biological functions of stress-responsive Vr-PLC3 in mung bean plants are discussed.

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36. In vivo localization in Arabidopsis protoplasts and root tissue.

Author

Lee MH, Lee Y, and Hwang I

Subjects
Arabidopsis ultrastructure, Arabidopsis Proteins ultrastructure, Plant Roots chemistry, Protoplasts metabolism, Molecular Biology methods, Plant Roots ultrastructure, Protoplasts ultrastructure
Abstract

In eukaryotic cells, a large number of proteins are transported to their final destination after translation by a process called intracellular trafficking. Transient gene expression, either in plant protoplasts or in specific plant tissues, is a fast, flexible, and reproducible approach to study the cellular function of proteins, protein subcellular localizations, and protein-protein interactions. Here we describe the general method of protoplast isolation, polyethylene glycol-mediated protoplast transformation and immunostaining of protoplast or intact root tissues for studying the localization of protein in Arabidopsis.

Published
2013
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37. A WD40 repeat protein, Arabidopsis Sec13 homolog 1, may play a role in vacuolar trafficking by controlling the membrane association of AtDRP2A.

Author

Lee MH, Lee SH, Kim H, Jin JB, Kim DH, and Hwang I

Subjects
Amino Acid Motifs, Amino Acid Sequence, Arabidopsis ultrastructure, Arabidopsis Proteins chemistry, Cell Nucleus metabolism, Dynamins chemistry, Golgi Apparatus metabolism, Molecular Sequence Data, Protein Structure, Tertiary, Protein Transport, Sequence Alignment, Two-Hybrid System Techniques, Arabidopsis metabolism, Arabidopsis Proteins metabolism, Arabidopsis Proteins physiology, Dynamins metabolism, Vacuoles metabolism
Abstract

Dynamin-related protein 2A (AtDRP2A, formally ADL6), a member of the dynamin family, is critical for protein trafficking from the TGN to the central vacuole. However, the mechanism controlling its activity is not well understood in plant cells. We isolated Arabidopsis sec13 homolog1 (AtSeh1) that interacts with AtDRP2A by a yeast two-hybrid screening. AtSeh1 has four WD40 motifs and amino acid sequence homology to Sec13, a component of COPII vesicles. Coimmunoprecipitation and protein pull-down experiments demonstrated specific interaction between AtSeh1 and AtDRP2A. AtSeh1 bound to the pleckstrin homology domain of AtDRP2A in competition with the C-terminal domain of the latter, and this resulted in inhibition of the interaction between AtDRP2A and PtdIns3P in vitro. AtSeh1 localized to multiple locations: the nucleus, the prevacuolar compartment and the Golgi complex. Based on these results we propose that AtSeh1 plays a role in regulating cycling of AtDRP2A between membrane-bound and soluble forms.

Published
2006

38. The Vr-PLC3 gene encodes a putative plasma membrane-localized phosphoinositide-specific phospholipase C whose expression is induced by abiotic stress in mung bean (Vigna radiata L.).

Author

Kim YJ, Kim JE, Lee JH, Lee MH, Jung HW, Bahk YY, Hwang BK, Hwang I, and Kim WT

Subjects
Amino Acid Sequence, Cell Membrane enzymology, Conserved Sequence, Gene Expression Profiling, Gene Expression Regulation, Plant, Isoenzymes biosynthesis, Isoenzymes genetics, Kinetics, Mannitol pharmacology, Molecular Sequence Data, Phosphoinositide Phospholipase C, Phylogeny, Plant Structures genetics, Plant Structures metabolism, RNA, Messenger genetics, RNA, Messenger metabolism, RNA, Plant genetics, RNA, Plant metabolism, Sequence Homology, Amino Acid, Sodium Chloride pharmacology, Fabaceae enzymology, Fabaceae genetics, Genes, Plant, Phosphatidylinositol Diacylglycerol-Lyase biosynthesis, Phosphatidylinositol Diacylglycerol-Lyase genetics
Abstract

Phosphoinositide-specific phospholipase C (PI-PLC) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate to generate inositol 1,4,5-trisphosphate and diacylglycerol, both of which act as secondary messengers in animal cells. In this report, we identified in Vigna radiata L. (mung bean) three distinct partial cDNAs (pVr-PLC1, pVr-PLC2, and pVr-PLC3), which encode forms of putative PI-PLC. All three Vr-PLC genes were transcriptionally active and displayed unique patterns of expression. The Vr-PLC1 and Vr-PLC2 transcripts were constitutively expressed to varying degrees in every tissue of mung bean plants examined. In contrast, the Vr-PLC3 mRNA level was very low under normal growth conditions and was rapidly induced in an abscisic acid-independent manner under environmental stress conditions (drought and high salinity). An isolated genomic clone, about 8.2 kb in length, showed that Vr-PLC1 and Vr-PLC3 are in tandem array in the mung bean genome. The predicted primary sequence of Vr-PLC3 (M(r)=67.4 kDa) is reminiscent of the delta-isoform of animal enzymes which contain core sequences found in typical PI-PLCs, such as the catalytic domain comprising X and Y motifs, a lipid-binding C2 domain, and the less conserved EF-hand domain. Results of in vivo targeting experiment using a green fluorescent protein (GFP) showed that the GFP-Vr-PLC3 fusion protein was localized primarily to the plasma membrane of the Arabidopsis protoplast. The C2 domain was essential for Vr-PLC3 to be targeted to the plasma membrane. The possible biological functions of stress-responsive Vr-PLC3 in mung bean plants are discussed.

Published
2004
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