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Apparent eukaryotic origin of glutamine synthetase II from the bacterium Bradyrhizobium japonicum

Nature volume 322, pages 568–570 (1986)Cite this article

Abstract

The Rhizobiaceae family of bacteria is characterized by the ability to form cortical hypertrophies on plants, and the ability to re-isolate the bacteria from these galls or nodules1.This family includes the genera Rhizobium, Bradyrhizobium, Agrobacterium and Phyllobactenum. Another unique feature of these bacteria is that they contain two forms of the enzyme glutamine synthetase, termed GSI and GSII2,3.GSI is typical of prokaryotic glutamine synthetases with respect to enzyme structure, the modulation of activity by post-translational modification, immunological cross-reactivity, and amino-acid sequence2,4,5.By contrast, GSII is distinct from all other known prokaryotic glutamine synthetases in structure and immunological reactivity, and is not known to be post-translationally modified. In these respects GSII is similar to eukaryotic glutamine synthetases6. We have isolated and characterized the gene encoding GSII, which we term glnII, from Bradyrhizobium japonicum, the soybean symbiont. We show here that the amino-acid sequence of GSII, as inferred from the gene sequence, is highly homologous to plant glutamine synthetases, suggesting that this bacterial gene is of eukaryotic origin.

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Authors and Affiliations

  1. Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan, 48824, USA

    Todd A. Carlson & Barry K. Chelm

  2. Department of Biochemistry, Michigan State University, East Lansing, Michigan, 48824, USA

    Todd A. Carlson

  3. Department of Microbiology and Public Health, Michigan State University, East Lansing, Michigan, 48824, USA

    Barry K. Chelm

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  1. Todd A. Carlson
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  2. Barry K. Chelm
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Carlson, T., Chelm, B. Apparent eukaryotic origin of glutamine synthetase II from the bacterium Bradyrhizobium japonicum. Nature 322, 568–570 (1986). https://doi.org/10.1038/322568a0

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