Rhizobium meliloti NodP and NodQ form a multifunctional sulfate- activating complex requiring GTP for activity

J. S. Schwedock, C. Liu, T. S. Leyh, S. R. Long

Research output: Contribution to journalArticle

65 Scopus citations

Abstract

The nodulation genes nodP and nodQ are required for production of Rhizobium meliloti nodulation (Nod) factors. These sulfated oligosaccharides act as morphogenic signals to alfalfa, the symbiotic host of R. meliloti. In previous work, we have shown that nodP and nodQ encode ATP sulfurylase, which catalyzes the formation of APS (adenosine 5'-phosphosulfate) and PP(i). In the subsequent metabolic reaction, APS is converted to PAPS (3'- phosphoadenosine 5'-phosphosulfate) by APS kinase. In Escherichia coli, cysD and cysN encode ATP sulfurylase; cysC encodes APS kinase. Here, we present genetic, enzymatic, and sequence similarity data demonstrating that nodP and nodQ encode both ATP sulfurylase and APS kinase activities and that these enzymes associate into a multifunctional protein complex which we designate the sulfate activation complex. We have previously described the presence of a putative GTP-binding site in the nodQ sequence. The present report also demonstrates that GTP enhances the rate of PAPS synthesis from ATP and sulfate (SO42-) by NodP and NodQ expressed in E. coli. Thus, GTP is implicated as a metabolic requirement for synthesis of the R. meliloti Nod factors.

Original languageEnglish (US)
Pages (from-to)7055-7064
Number of pages10
JournalJournal of Bacteriology
Volume176
Issue number22
DOIs
StatePublished - 1994
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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