ArticleJournal of bacteriology2010
Mutagenesis and functional characterization of the four domains of GlnD, a bifunctional nitrogen sensor protein.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- The activation ofPlant direct · 2024Article
- Genome-Scale Investigation of the Regulation of azoR Expression in Escherichia coli Using Computational Analysis and Transposon Mutagenesis.Microbial ecology · 2024Article
- Arabidopsis ACT DOMAIN REPEAT9 represses glucose signaling pathways.Plant physiology · 2023Article
- Transient mutation bias increases the predictability of evolution on an empirical genotype-phenotype landscape.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Article
- Evolution and diversification of the ACT-like domain associated with plant basic helix-loop-helix transcription factors.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The coralScience advances · 2022Article
- SNAT7 regulates mTORC1 via macropinocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Spontaneous Phage Resistance in Avian PathogenicFrontiers in microbiology · 2021Article
- Manipulating nitrogen regulation in diazotrophic bacteria for agronomic benefit.Biochemical Society transactions · 2019Review
- Protein Activity Sensing in Bacteria in Regulating Metabolism and Motility.Frontiers in microbiology · 2019Review
- The uridylyltransferase GlnD and tRNA modification GTPase MnmE allosterically controlThe Journal of biological chemistry · 2018Article
- Growth Adaptation ofFrontiers in microbiology · 2018Article
- GlnK Facilitates the Dynamic Regulation of Bacterial Nitrogen Assimilation.Biophysical journal · 2017Article
- Glutamine rapidly induces the expression of key transcription factor genes involved in nitrogen and stress responses in rice roots.BMC genomics · 2015Article
- Purification, crystallization and preliminary X-ray analysis of a putative nucleotide phosphohydrolase, YpgQ, from Bacillus subtilis.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Post-translational modification of P II signal transduction proteins.Frontiers in microbiology · 2014Review
- Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective.Microbiology and molecular biology reviews : MMBR · 2013Review
- Sensitivity and robustness in covalent modification cycles with a bifunctional converter enzyme.Biophysical journal · 2013Article
- Nitrogen regulation of protein-protein interactions and transcript levels of GlnK PII regulator and AmtB ammonium transporter homologs in Archaea.MicrobiologyOpen · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
GlnD is a bifunctional uridylyltransferase/uridylyl-removing enzyme (UTase/UR) and is believed to be the primary sensor of nitrogen status in the cell by sensing the level of glutamine in enteric bacteria. It plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of P(II) protein; P(II) in turn regulates a variety of other proteins. GlnD appears to have four distinct domains: an N-terminal nucleotidyltransferase (NT) domain; a central HD domain, named after conserved histidine and aspartate residues; and two C-terminal ACT domains, named after three of the allosterically regulated enzymes in which this domain is found. Here we report the functional analysis of these domains of GlnD from Escherichia coli and Rhodospirillum rubrum. We confirm the assignment of UTase activity to the NT domain and show that the UR activity is a property specifically of the HD domain: substitutions in this domain eliminated UR activity, and a truncated protein lacking the NT domain displayed UR activity. The deletion of C-terminal ACT domains had little effect on UR activity itself but eliminated the ability of glutamine to stimulate that activity, suggesting a role for glutamine sensing by these domains. The deletion of C-terminal ACT domains also dramatically decreased UTase activity under all conditions tested, but some of these effects are due to the competition of UTase activity with unregulated UR activity in these variants.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.