Sequence of the Bacillus subtilis glutamine synthetase gene region

Strauch, Mark A.; Aronson, Arthur I.; Brown, Stuart; Schreier, Harold J.; Sonenshein, Abraham L.

doi:10.1016/0378-1119(88)90042-x

Cited by 68 publications

(51 citation statements)

References 34 publications

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“…GS is a large protein (M r of 600,000) that contains 12 identical subunits (10,11). A ternary complex among FBI-GS, GlnR, and DNA would have a significantly lower mobility than the GlnR-DNA complex in this assay.…”

Section: Fbi-gs Does Not Form a Stable Complex With Glnrmentioning

confidence: 99%

“…Although the primary and quaternary structures of the enteric and B. subtilis GS are remarkably similar (10,11), the activity of B. subtilis GS, but not enteric GS, is subject to feedback inhibition by glutamine (12). The GS-dependent regulation of TnrA activity has been shown to result from the feedback-inhibited form of GS (FBI-GS), forming a protein-protein complex with TnrA that inhibits the DNA-binding activity of TnrA (13).…”

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confidence: 99%

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Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR–DNA complexes

Fisher

Wray

2008

Proc. Natl. Acad. Sci. U.S.A.

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The Bacillus subtilis GlnR repressor controls gene expression in response to nitrogen availability. Because all GlnR-regulated genes are expressed constitutively in mutants lacking glutamine synthetase (GS), GS is required for repression by GlnR. Feedbackinhibited GS (FBI-GS) was shown to activate GlnR DNA binding with an in vitro electophoretic mobility shift assay (EMSA). The activation of GlnR DNA binding by GS in these experiments depended on the feedback inhibitor glutamine and did not occur with mutant GS proteins defective in regulating GlnR activity in vivo. Although stable GS-GlnR-DNA ternary complexes were not observed in the EMSA experiments, cross-linking experiments showed that a protein-protein interaction occurs between GlnR and FBI-GS. This interaction was reduced in the absence of the feedback inhibitor glutamine and with mutant GS proteins. Because FBI-GS significantly reduced the dissociation rate of the GlnR-DNA complexes, the stability of these complexes is enhanced by FBI-GS. These results argue that FBI-GS acts as a chaperone that activates GlnR DNA binding through a transient protein-protein interaction that stabilizes GlnR-DNA complexes. GS was shown to control the activity of the B. subtilis nitrogen transcription factor TnrA by forming a stable complex between FBI-GS and TnrA that inhibits TnrA DNA binding. Thus, B. subtilis GS is an enzyme with dual catalytic and regulatory functions that uses distinct mechanisms to control the activity of two different transcription factors.nitrogen regulation ͉ MerR ͉ TurA

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Section: Fbi-gs Does Not Form a Stable Complex With Glnrmentioning

confidence: 99%

mentioning

confidence: 99%

Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR–DNA complexes

Fisher

Wray

2008

Proc. Natl. Acad. Sci. U.S.A.

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“…GlnR of B. subtilis [20], MerR of various eubacteria [21] and TipAL of Streptomyces lividans [22], all transcriptional regulators of gene expression exhibit significant homology in the N-terminal region. The segment of ScgR from residues 16 to 79 had 52, 35 and 37% identity with a corresponding segment of GlnR, MerR (Thiobacillusferrooxidans) and TipAL, respectively (Fig.…”

Section: Cloning Of a Novel Transcriptional Regulator Frommentioning

confidence: 99%

The secG deletion mutation of Escherichia coli is suppressed by expression of a novel regulatory gene of Bacillus subtilis

1996

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“…The GlnR protein is active during growth with excess nitrogen (5)(6)(7)(8). Although genetic experiments have shown that GS is required for GlnR-dependent gene regulation, the precise role of GS in GlnR regulation has yet to be determined (7,9).…”

mentioning

confidence: 99%

A Feedback-resistant Mutant of Bacillus subtilis Glutamine Synthetase with Pleiotropic Defects in Nitrogen-regulated Gene Expression

Wray

Fisher

2005

Journal of Biological Chemistry

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The Bacillus subtilis TnrA transcription factor regulates gene expression during nitrogen-limited growth. When cells are grown with excess nitrogen, feedback-inhibited glutamine synthetase forms a protein-protein complex with TnrA and prevents TnrA from binding to DNA. A mutation in glutamine synthetase with a phenylalanine replacement at the Ser-186 residue (S186F) was isolated by screening for B. subtilis mutants with constitutive TnrA activity. Although S186F glutamine synthetase has kinetic properties that are similar to the wild-type protein, the S186F enzyme is resistant to feedback inhibition by glutamine and AMP. Ligand binding experiments revealed that the S186F protein had a lower affinity for glutamine and AMP than the wild-type enzyme. S186F glutamine synthetase was defective in its ability to block DNA binding by TnrA in vitro. The properties of the feedback-resistant S186F mutant support the model in which the feedback-inhibited form of glutamine synthetase regulates TnrA activity in vivo.

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Sequence of the Bacillus subtilis glutamine synthetase gene region

Cited by 68 publications

References 34 publications

Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR–DNA complexes

Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR–DNA complexes

The secG deletion mutation of Escherichia coli is suppressed by expression of a novel regulatory gene of Bacillus subtilis

A Feedback-resistant Mutant of Bacillus subtilis Glutamine Synthetase with Pleiotropic Defects in Nitrogen-regulated Gene Expression

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