Uridylylation of the P<sub>II</sub> protein in <i>Rhizobium leguminosarum</i>

Colonna-Romano, Sergio; Patriarca, Eduardo J.; Amar, Mohamed S; Bernard, P; Manco, Giuseppe; Lamberti, Alessandro; laccarino, Maurizio; Defez, Roberto

doi:10.1016/0014-5793(93)80927-m

Cited by 27 publications

(25 citation statements)

References 20 publications

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“…This residue is highly conserved, being present in the GlnB and GlnK proteins of the proteobacteria and the actinobacteria. Uridylylation of P II proteins has been demonstrated in Rhizobium leguminosarum (40), Klebsiella pneumoniae (55), Azospirillum brasilense (47,50), Azotobacter vinelandii (196), Herbaspirillum seropedicae (20), and Azoarcus sp. strain BH72 (150) and suggested in Sinorhizobium meliloti (8) (114), and Corynebacterium glutamicum (104).…”

Section: Modification Of P II In Response To Nitrogenmentioning

confidence: 99%

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

Arcondéguy

Jack

Merrick

2001

Microbiol Mol Biol Rev

398

456

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SUMMARY The PII family of signal transduction proteins are among the most widely distributed signal proteins in the bacterial world. First identified in 1969 as a component of the glutamine synthetase regulatory apparatus, PII proteins have since been recognized as playing a pivotal role in control of prokaryotic nitrogen metabolism. More recently, members of the family have been found in higher plants, where they also potentially play a role in nitrogen control. The PII proteins can function in the regulation of both gene transcription, by modulating the activity of regulatory proteins, and the catalytic activity of enzymes involved in nitrogen metabolism. There is also emerging evidence that they may regulate the activity of proteins required for transport of nitrogen compounds into the cell. In this review we discuss the history of the PII proteins, their structures and biochemistry, and their distribution and functions in prokaryotes. We survey data emerging from bacterial genome sequences and consider other likely or potential targets for control by PII proteins.

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Section: Modification Of P II In Response To Nitrogenmentioning

confidence: 99%

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

Arcondéguy

Jack

Merrick

2001

Microbiol Mol Biol Rev

398

456

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“…In fact, P II is involved in the covalent (and reversible) modification of both NtrC (through phosphorylation) and GSI (adenylylation), and thus in the regulation of their activity (5,31,32,74,75). In S. meliloti, B. japonicum, and R. leguminosarum, glnB is cotranscribed with glnA (GSI), forming a glnBA operon.…”

Section: P II Regulatory Proteinmentioning

confidence: 99%

“…Hence, glnB expression in R. leguminosarum is N regulated (fourfold lower in NH 4 ϩ compared to NO 3 Ϫ ), while it is constitutive in enteric bacteria (for a review, see reference 84). The P II proteins of R. leguminosarum and S. meliloti, as in enteric bacteria, are subject to covalent uridylylation, which modulates their activity (6,32,159). The degree of uridylylation is high under N limitation and undetectable under N excess (32).…”

Section: P II Regulatory Proteinmentioning

confidence: 99%

Key Role of Bacterial NH ₄ ⁺ Metabolism in Rhizobium-Plant Symbiosis

Patriarca

Tatè

Iaccarino

2002

Microbiol Mol Biol Rev

159

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Symbiotic nitrogen fixation is carried out in specialized organs, the nodules, whose formation is induced on leguminous host plants by bacteria belonging to the family Rhizobiaceae. Nodule development is a complex multistep process, which requires continued interaction between the two partners and thus the exchange of different signals and metabolites. NH4+ is not only the primary product but also the main regulator of the symbiosis: either as ammonium and after conversion into organic compounds, it regulates most stages of the interaction, from the production of nodule inducers to the growth, function, and maintenance of nodules. This review examines the adaptation of bacterial NH4+ metabolism to the variable environment generated by the plant, which actively controls and restricts bacterial growth by affecting oxygen and nutrient availability, thereby allowing a proficient interaction and at the same time preventing parasitic invasion. We describe the regulatory circuitry responsible for the downregulation of bacterial genes involved in NH4+ assimilation occurring early during nodule invasion. This is a key and necessary step for the differentiation of N2-fixing bacteroids (the endocellular symbiotic form of rhizobia) and for the development of efficient nodules

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“…The assay for P II uridylylation was performed according to Colonna-Romano et al (1993). Strains were grown in minimal media (RMM) containing glutamate as a nitrogen source.…”

Section: Construction Of Mutant Strains and Recombinant Plasmidsmentioning

confidence: 99%

“…Expression of the glnII gene, which is preceded by a characteristic σ&%-dependent promoter, is strictly regulated by NtrB\NtrC and most probably turned off in symbiosis (Shatters et al, 1989). It was shown that the P II protein, which is encoded upstream of glnA (Chiurazzi & Iaccarino, 1990), negatively controls the transcriptional activity of NtrC and that it is subject to uridylylation, suggesting the presence of a UTase\UR-activity also in R. leguminosarum (Amar et al, 1994 ;Colonna-Romano et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation

et al. 2000

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A Rhizobium leguminosarum bv. viciae VF39 gene (glnD) encoding the uridylyltransferase/uridylyl-removing enzyme, which constitutes the sensory component of the nitrogen regulation (ntr) system, was identified, cloned and characterized. The deduced amino acid sequence contains the conserved active site motif of the nucleotidyltransferase superfamily and is highly homologous to the glnD gene products of other bacterial species. Downstream of the VF39 glnD resides an open reading frame with similarity to the Salmonella typhimurium virulence factor gene mviN. Mutation of the glnD gene abolished the ability to use nitrate as a sole nitrogen source but not glutamine. In addition, neither uridylylation of P II nor induction of the ntr-regulated glnII gene (encoding glutamine synthetase II) under ammonium deficiency could be observed in mutant strains. This strongly suggests that glnD mutants harbour a permanently deuridylylated P II protein and as a consequence are unable to activate transcription from NtrC-dependent promoters. The glnD gene itself is expressed constitutively, irrespective of the nitrogen content of the medium. A functional GlnD protein is not essential for nitrogen fixation in R. leguminosarum bv. viciae, but in situ detection of glnD expression in the symbiotic and infection zone of the root nodule and quantitative measurements suggest that at least part of the ntr system functions in symbiosis. The results also indicate that the N-terminal part of GlnD is essential for the cell, as deletions in the 5'-region of the gene appear to be lethal and mutations possibly affecting the expression of the first half of the protein have a significant effect on the vitality of the mutant strain.

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Uridylylation of the P_II protein in Rhizobium leguminosarum

Cited by 27 publications

References 20 publications

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

Key Role of Bacterial NH ₄ ⁺ Metabolism in Rhizobium-Plant Symbiosis

The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation

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Uridylylation of the PII protein in Rhizobium leguminosarum

Cited by 27 publications

References 20 publications

PIISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

PIISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

Key Role of Bacterial NH 4 + Metabolism in Rhizobium-Plant Symbiosis

The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation

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Uridylylation of the P_II protein in Rhizobium leguminosarum

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

Key Role of Bacterial NH ₄ ⁺ Metabolism in Rhizobium-Plant Symbiosis