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

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

Research output: Contribution to journalArticle

64 Citations (Scopus)

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
StatePublished - 1994
Externally publishedYes

Fingerprint

adenylylsulfate kinase
Sulfate Adenylyltransferase
Sinorhizobium meliloti
Adenosine Phosphosulfate
Guanosine Triphosphate
Phosphoadenosine Phosphosulfate
Sulfates
Escherichia coli
Medicago sativa
Oligosaccharides
Adenosine Triphosphate
Binding Sites
Enzymes
Genes
Proteins

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Rhizobium meliloti NodP and NodQ form a multifunctional sulfate- activating complex requiring GTP for activity. / Schwedock, J. S.; Liu, C.; Leyh, Thomas S.; Long, S. R.

In: Journal of Bacteriology, Vol. 176, No. 22, 1994, p. 7055-7064.

Research output: Contribution to journalArticle

@article{9df5ec20791e4c0a8234efcb94ca2faa,
title = "Rhizobium meliloti NodP and NodQ form a multifunctional sulfate- activating complex requiring GTP for activity",
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.",
author = "Schwedock, {J. S.} and C. Liu and Leyh, {Thomas S.} and Long, {S. R.}",
year = "1994",
language = "English (US)",
volume = "176",
pages = "7055--7064",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "22",

}

TY - JOUR

T1 - Rhizobium meliloti NodP and NodQ form a multifunctional sulfate- activating complex requiring GTP for activity

AU - Schwedock, J. S.

AU - Liu, C.

AU - Leyh, Thomas S.

AU - Long, S. R.

PY - 1994

Y1 - 1994

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0028130514&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028130514&partnerID=8YFLogxK

M3 - Article

C2 - 7961471

AN - SCOPUS:0028130514

VL - 176

SP - 7055

EP - 7064

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 22

ER -