Preliminary X-ray diffraction analysis of crystals of the PII protein from Escherichia coli

Mel, V. Srini J. De; Kamberov, Emmanuel S.; Martin, Philip D.; Zhang, Jun; Ninfa, Alexander J.; Edwards, Brian F.P.

doi:10.1016/0022-2836(94)90049-3

Cited by 11 publications

(11 citation statements)

References 16 publications

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“…However, subsequent crystallization studies and sedimentation equilibrium experiments have shown that it is in fact a trimer (33,46,236). The molecular mass of the P II monomer was elucidated by matrix-assisted laser desorption mass spectrometry and shown to be 12,435 Da, which agrees very well with the prediction from the DNA sequence of 12,427 Da (235,236).…”

Section: Biochemistry Of P II Proteinssupporting

confidence: 71%

“…The second gene encodes a protein similar to GlnK and is linked to an amtB homologue (125,157,182,185,222,254) (Y. Zhang and G. Roberts, personal communication). One exception to this pattern is Azospirillum brasilense, in which the glnK-like gene (termed glnZ) is not linked to amtB (46,49,228), but instead an open reading frame encoding a protein with 26% identity to the aspartate aminotransferase of Bacillus subtilis is found just 300 bp downstream of glnZ (47). The second exception is Acetobacter diazotrophicus, which has both a glnB-glnA operon and two glnK-amtB operons (D. Meletzus, personal communication).…”

Section: ␣ Proteobacteriamentioning

confidence: 99%

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P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

Arcondéguy

Jack

Merrick

2001

Microbiol Mol Biol Rev

397

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: Biochemistry Of P II Proteinssupporting

confidence: 71%

Section: ␣ Proteobacteriamentioning

confidence: 99%

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

Arcondéguy

Jack

Merrick

2001

Microbiol Mol Biol Rev

397

456

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“…From results based on gel filtration (124) and combined native and SDS-polyacrylamide gel electrophoresis, it was concluded that GlnB consists of four identical subunits (149). However, after sedimentation equilibrium analysis (150) and preliminary X-ray diffraction analysis (150,151), it was concluded that GlnB was a homotrimer instead of a homotetramer. This was confirmed by resolving the structure of nonuridylylated GlnB at a high resolution through X-ray diffraction analyses (152,153).…”

Section: Glnbmentioning

confidence: 99%

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

Heeswijk¹,

Westerhoff

Boogerd³

2013

Microbiol Mol Biol Rev

228

246

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SUMMARY We present a comprehensive overview of the hierarchical network of intracellular processes revolving around central nitrogen metabolism in Escherichia coli . The hierarchy intertwines transport, metabolism, signaling leading to posttranslational modification, and transcription. The protein components of the network include an ammonium transporter (AmtB), a glutamine transporter (GlnHPQ), two ammonium assimilation pathways (glutamine synthetase [GS]-glutamate synthase [glutamine 2-oxoglutarate amidotransferase {GOGAT}] and glutamate dehydrogenase [GDH]), the two bifunctional enzymes adenylyl transferase/adenylyl-removing enzyme (ATase) and uridylyl transferase/uridylyl-removing enzyme (UTase), the two trimeric signal transduction proteins (GlnB and GlnK), the two-component regulatory system composed of the histidine protein kinase nitrogen regulator II (NRII) and the response nitrogen regulator I (NRI), three global transcriptional regulators called nitrogen assimilation control (Nac) protein, leucine-responsive regulatory protein (Lrp), and cyclic AMP (cAMP) receptor protein (Crp), the glutaminases, and the nitrogen-phosphotransferase system. First, the structural and molecular knowledge on these proteins is reviewed. Thereafter, the activities of the components as they engage together in transport, metabolism, signal transduction, and transcription and their regulation are discussed. Next, old and new molecular data and physiological data are put into a common perspective on integral cellular functioning, especially with the aim of resolving counterintuitive or paradoxical processes featured in nitrogen assimilation. Finally, we articulate what still remains to be discovered and what general lessons can be learned from the vast amounts of data that are available now.

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“…Quoted molarities refer to the GS dodecamer, ATase monomer, and P II /GlnK trimer de Mel et al, 1994;Carr et al, 1996). The adenylylation reaction was monitored by the formation of g -glutamylhydroxamate determined by the g -glutamyl transferase assay (Stadtman et al, 1979), performed in microtitre plates.…”

Section: In Vitro Adenylylation Reactionsmentioning

confidence: 99%

An alternative P_II protein in the regulation of glutamine synthetase in Escherichia coli

Heeswijk

Hoving

Molenaar

et al. 1996

Molecular Microbiology

198

291

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SummaryThe P II protein has been considered pivotal to the dual cascade regulating ammonia assimilation through glutamine synthetase activity. Here we show that P II , encoded by the glnB gene, is not always essential; for instance upon ammonia deprivation of a glnB deletion strain, glutamine synthetase can be deadenylylated as effectively as in the wild-type strain. We describe a new operon, glnK amtB, which encodes a homologue of P II and a putative ammonia transporter. We cloned and overexpressed glnK and found that the expressed protein had almost the same molecular weight as P II , reacted with polyclonal P II antibody, and was 67% identical in terms of amino acid sequence with Escherichia coli P II . Like P II , purified GlnK can activate the adenylylation of glutamine synthetase in vitro, and, in vivo, the GlnK protein is uridylylated in a glnD-dependent fashion. Unlike P II , however, the expression of glnK depends on the presence of UTase, nitrogen regulator I (NRI), and absence of ammonia. Because of a NRI and a r N (r 54 ) RNA polymerase-binding consensus sequence upstream from the glnK gene, this suggests that glnK is regulated through the NRI/ NRII two-component regulatory system. Indeed, in cells grown in the presence of ammonia, glutamine synthetase deadenylylation upon ammonia depletion depended on P II . Possible regulatory implications of this conditional redundancy of P II are discussed.

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Preliminary X-ray diffraction analysis of crystals of the PII protein from Escherichia coli

Cited by 11 publications

References 16 publications

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

An alternative P_II protein in the regulation of glutamine synthetase in Escherichia coli

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Preliminary X-ray diffraction analysis of crystals of the PII protein from Escherichia coli

Cited by 11 publications

References 16 publications

PIISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

PIISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

An alternative PII protein in the regulation of glutamine synthetase in Escherichia coli

Contact Info

Product

Resources

About

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

P_IISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control

An alternative P_II protein in the regulation of glutamine synthetase in Escherichia coli