Lethality of glnD null mutations in Azotobacter vinelandii is suppressible by prevention of glutamine synthetase adenylylation

Microbiology
R ColnaghiC Kennedy

Abstract

GlnD is a pivotal protein in sensing intracellular levels of fixed nitrogen and has been best studied in enteric bacteria, where it reversibly uridylylates two related proteins, PII and GlnK. The uridylylation state of these proteins determines the activities of glutamine synthetase (GS) and NtrC. Results presented here demonstrate that glnD is an essential gene in Azotobacter vinelandii. Null glnD mutations were introduced into the A. vinelandii genome, but none could be stably maintained unless a second mutation was present that resulted in unregulated activity of GS. One mutation, gln-71, occurred spontaneously to give strain MV71, which failed to uridylylate the GlnK protein. The second, created by design, was glnAY407F (MV75), altering the adenylylation site of GS. The gln-71 mutation is probably located in glnE, encoding adenylyltransferase, because introducing the Escherichia coli glnE gene into MV72, a glnD(+) derivative of MV71, restored the regulation of GS activity. GlnK-UMP is therefore apparently required for GS to be sufficiently deadenylylated in A. vinelandii for growth to occur. The DeltaglnD GS(c) isolates were Nif(-), which could be corrected by introducing a nifL mutation, confirming a role for GlnD in media...Continue Reading

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Citations

Aug 7, 2012·FEMS Microbiology Reviews·Luciano F HuergoMike Merrick
Nov 10, 2004·Proceedings of the National Academy of Sciences of the United States of America·Isabel Martinez-ArgudoRay Dixon
Jul 21, 2004·Nature Reviews. Microbiology·Ray Dixon, Daniel Kahn
Apr 23, 2017·Applied and Environmental Microbiology·Florence MusJohn W Peters
Nov 15, 2011·Molecular Plant-microbe Interactions : MPMI·Svetlana N YurgelMichael L Kahn
Jan 16, 2002·Journal of Bacteriology·Paul RudnickChristina Kennedy
Mar 10, 2021·Applied Microbiology and Biotechnology·Rafael Ambrosio, Leonardo Curatti

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