Abstract
The transcription of sigma 54 RNA polymerase-dependent nitrogen-regulated genes is activated by nitrogen regulator I (NRI)-phosphate. The kinase NRII is responsible for the phosphorylation of NRI. It has been shown that NRII also has the ability to dephosphorylate NRI-phosphate but only when PII is present at a concentration greatly in excess of that of NRII. We have now shown that glutamate enables PII to stimulate the dephosphorylation of NRI-phosphate when present in equimolar concentration with NRII. This effect of glutamate appears to be a backup control that becomes effective when the normal regulation of PII activity is disabled.
MeSH Terms
Bacterial Proteins/drug effects,metabolism
Cobalt/pharmacology
DNA-Binding Proteins/metabolism
DNA-Directed RNA Polymerases/metabolism
Dose-Response Relationship, Drug
Escherichia coli/enzymology,metabolism
Escherichia coli Proteins
Gene Expression Regulation, Bacterial
Glutamate-Ammonia Ligase/biosynthesis
Glutamic Acid/pharmacology
Ketoglutaric Acids/pharmacology
PII Nitrogen Regulatory Proteins
Phosphorylation
Protein Kinases/metabolism
RNA Polymerase Sigma 54
Sigma Factor/metabolism
Trans-Activators
Transcription Factors
Chemicals
Bacterial Proteins
DNA-Binding Proteins
Escherichia coli Proteins
Ketoglutaric Acids
PII Nitrogen Regulatory Proteins
Sigma Factor
Trans-Activators
Transcription Factors
glnG protein, E coli
rpoN protein, E coli
Cobalt
Glutamic Acid
PIID regulatory protein, Bacteria
Protein Kinases
DNA-Directed RNA Polymerases
RNA Polymerase Sigma 54
Glutamate-Ammonia Ligase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Liu J
Department of Biology, Massachusetts Institute of Technology, Cambridge, 02139.
Magasanik B
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15 references, click to expand
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