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New Phytol. 2011 Apr;190(1):35-48. doi: 10.1111/j.1469-8137.2010.03581.x. Epub 2010 Dec 22.

An elaborate heterotrimeric G-protein family from soybean expands the diversity of plant G-protein networks.

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1
Donald Danforth Plant Science Center, 975 North Warson Road, St Louis, MO 63132, USA Department of Biology, Washington University, One Brookings Drive, Campus Box 1137, St Louis, MO 63130, USA.

Abstract

The repertoire of heterotrimeric G-proteins in plant species analyzed thus far is simple, with the presence of only two possible canonical heterotrimers in Arabidopsis and rice vs hundreds in animal systems. We assessed whether genome duplication events have resulted in the multiplicity of G-protein in plant species like soybean that would increase the complexity of G-protein networks. We identified and amplified four Gα, four Gβ and two Gγ proteins, analyzed their expression profile by quantitative PCR during different developmental stages. We purified the four Gα proteins and analyzed their guanosine-5'-triphosphate (GTP)-binding and GTPase activity. We performed yeast-based interaction analysis to assess the interaction specificity of different G-protein subunits. Our results show that all 10 G-protein genes are retained in the soybean genome and ubiquitously expressed. The four Gα proteins seem to be plasma membrane-localized. The G-protein genes have interesting expression profiles during seed development and germination. The four Gα proteins form two distinct groups based on their GTPase activity. Yeast-based interaction analyses predict that the proteins interact in most of the possible combinations, with some degree of interaction specificity between duplicated gene pairs. This research identifies the most elaborate heterotrimeric G-protein network known to date in the plant kingdom.

KEYWORDS:

GTP-binding; GTPase activity; genome duplication; heterotrimeric G-proteins; protein-protein interaction; soybean (Glycine max)

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