Characterization of Heterotrimeric G Protein γ4 Subunit in Rice

Heterotrimeric G proteins are the molecule switch that transmits information from external signals to intracellular target proteins in mammals and yeast cells. In higher plants, heterotrimeric G proteins regulate plant architecture. Rice harbors one canonical &#945; subunit gene (<i>RGA1&l...

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Bibliographic Details
Main Authors: Sakura Matsuta, Aki Nishiyama, Genki Chaya, Takafumi Itoh, Kotaro Miura, Yukimoto Iwasaki
Format: Article
Language:English
Published: MDPI AG 2018-11-01
Series:International Journal of Molecular Sciences
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Online Access:https://www.mdpi.com/1422-0067/19/11/3596
Description
Summary:Heterotrimeric G proteins are the molecule switch that transmits information from external signals to intracellular target proteins in mammals and yeast cells. In higher plants, heterotrimeric G proteins regulate plant architecture. Rice harbors one canonical &#945; subunit gene (<i>RGA1</i>), four extra-large GTP-binding protein genes (XLGs), one canonical &#946;-subunit gene (<i>RGB1</i>), and five &#947;-subunit genes (tentatively designated <i>RGG1</i>, <i>RGG2</i>, <i>RGG3</i>/<i>GS3</i>/<i>Mi</i>/<i>OsGGC1</i>, <i>RGG4</i>/<i>DEP1</i>/<i>DN1</i>/<i>qPE9-1</i>/<i>OsGGC3</i>, and <i>RGG5</i>/<i>OsGGC2</i>) as components of the heterotrimeric G protein complex. Among the five &#947;-subunit genes, <i>RGG1</i> encodes the canonical &#947;-subunit, <i>RGG2</i> encodes a plant-specific type of &#947;-subunit with additional amino acid residues at the N-terminus, and the remaining three &#947;-subunit genes encode atypical &#947;-subunits with cysteine-rich C-termini. We characterized the <i>RGG4</i>/<i>DEP1</i>/<i>DN1</i>/<i>qPE9-1</i>/<i>OsGGC3</i> gene product G&#947;4 in the wild type (WT) and truncated protein G&#947;4∆Cys in the <i>RGG4</i>/<i>DEP1</i>/<i>DN1</i>/<i>qPE9-1</i>/<i>OsGGC3</i> mutant, <i>Dn1-1</i>, as littele information regarding the native G&#947;4 and G&#947;4∆Cys proteins is currently available. Based on liquid chromatography-tandem mass spectrometry analysis, immunoprecipitated G&#947;4 candidates were confirmed as actual G&#947;4. Similar to &#945;-(G&#945;) and &#946;-subunits (G&#946;), G&#947;4 was enriched in the plasma membrane fraction and accumulated in the developing leaf sheath. As <i>RGG4</i>/<i>DEP1</i>/<i>DN1</i>/<i>qPE9-1</i>/<i>OsGGC3</i> mutants exhibited dwarfism, tissues that accumulated G&#947;4 corresponded to the abnormal tissues observed in <i>RGG4</i>/<i>DEP1</i>/<i>DN1</i>/<i>qPE9-1</i>/<i>OsGGC3</i> mutants.
ISSN:1422-0067