ArticlePLoS pathogens2015
The aspartate-less receiver (ALR) domains: distribution, structure and function.
Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Widespread atypical response regulator SecR governs bacterial growth on methylamines through the serine cycle.Communications biology · 2026Article
- A clarifying perspective on bacterial pseudo-receiver domains.Journal of bacteriology · 2025Review
- Characterization of two co-regulated response regulators inJournal of bacteriology · 2025Article
- FrzS acts as a polar beacon to recruit SgmX, a central activator of type IV pili during Myxococcus xanthus motility.The EMBO journal · 2023Article
- Promoter DNA recognition by theFrontiers in molecular biosciences · 2023Article
- A large-scale genetic screen identifies genes essential for motility in Agrobacterium fabrum.PloS one · 2023Article
- Motility control through an anti-activation mechanism in Agrobacterium tumefaciens.Molecular microbiology · 2021Article
- Predicted Functional and Structural Diversity of Receiver Domains in Fungal Two-Component Regulatory Systems.mSphere · 2021Article
- Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation.Journal of bacteriology · 2020Article
- Phase variation of a signal transduction system controls Clostridioides difficile colony morphology, motility, and virulence.PLoS biology · 2019Article
- RitR is an archetype for a novel family of redox sensors in the streptococci that has evolved from two-component response regulators and is required for pneumococcal colonization.PLoS pathogens · 2018Article
- Role of CovR phosphorylation in gene transcription in Streptococcus mutans.Microbiology (Reading, England) · 2018Article
- Non-canonical activation of OmpR drives acid and osmotic stress responses in single bacterial cells.Nature communications · 2017Article
- The Atypical Response Regulator AtvR Is a New Player in Pseudomonas aeruginosa Response to Hypoxia and Virulence.Infection and immunity · 2017Article
- Perturbation of manganese metabolism disrupts cell division in Streptococcus pneumoniae.Molecular microbiology · 2017Article
- To ∼P or Not to ∼P? Non-canonical activation by two-component response regulators.Molecular microbiology · 2017Review
- Experimental Analysis of Functional Variation within Protein Families: Receiver Domain Autodephosphorylation Kinetics.Journal of bacteriology · 2016Article
- Correction: The Aspartate-Less Receiver (ALR) Domains: Distribution, Structure and Function.PLoS pathogens · 2015Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Two-component signaling systems are ubiquitous in bacteria, Archaea and plants and play important roles in sensing and responding to environmental stimuli. To propagate a signaling response the typical system employs a sensory histidine kinase that phosphorylates a Receiver (REC) domain on a conserved aspartate (Asp) residue. Although it is known that some REC domains are missing this Asp residue, it remains unclear as to how many of these divergent REC domains exist, what their functional roles are and how they are regulated in the absence of the conserved Asp. Here we have compiled all deposited REC domains missing their phosphorylatable Asp residue, renamed here as the Aspartate-Less Receiver (ALR) domains. Our data show that ALRs are surprisingly common and are enriched for when attached to more rare effector outputs. Analysis of our informatics and the available ALR atomic structures, combined with structural, biochemical and genetic data of the ALR archetype RitR from Streptococcus pneumoniae presented here suggest that ALRs have reorganized their active pockets to instead take on a constitutive regulatory role or accommodate input signals other than Asp phosphorylation, while largely retaining the canonical post-phosphorylation mechanisms and dimeric interface. This work defines ALRs as an atypical REC subclass and provides insights into shared mechanisms of activation between ALR and REC domains.
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Registered trials
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.