ArticleNature structural & molecular biology2011
Structural basis for the molecular evolution of SRP-GTPase activation by protein.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 64 citations in OpenAlex.
- Where and how many: evolutionary diversification of a molecular switch regulating flagellar patterns.Journal of bacteriology · 2026Review
- Role of FlhF and its domains in the assembly of a polar flagellum inJournal of bacteriology · 2025Article
- FlhG Cooperates With the Cell Cycle Regulator GpsB to Confine Peritrichous Flagella in B. subtilis.Molecular microbiology · 2025Article
- Article
- Polar confinement of a macromolecular machine by an SRP-type GTPase.Nature communications · 2024Article
- Structure of the GDP-bound state of the SRP GTPase FlhF.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Control of the flagellation pattern inJournal of bacteriology · 2023Article
- Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.Nature communications · 2022Article
- Role of the major determinant of polar flagellation FlhG in the endoflagella-containing spirochete Leptospira.Molecular microbiology · 2021Article
- Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle.Cell reports · 2021Article
- The very early evolution of protein translocation across membranes.PLoS computational biology · 2021Article
- Architecture and regulation of an enterobacterial cellulose secretion system.Science advances · 2021Article
- Interdependent Polar Localization of FlhF and FlhG and Their Importance for Flagellum Formation ofFrontiers in microbiology · 2021Article
- An ATP-dependent partner switch links flagellar C-ring assembly with gene expression.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- FlhF regulates the number and configuration of periplasmic flagella in Borrelia burgdorferi.Molecular microbiology · 2020Article
- Assembly mechanism of a supramolecular MS-ring complex to initiate bacterial flagellar biogenesis inJournal of bacteriology · 2020Article
- Regulation of the Single Polar Flagellar Biogenesis.Biomolecules · 2020Review
- Article
- Article
- Signal Recognition Particle RNA Contributes to Oxidative Stress Response inFrontiers in microbiology · 2020Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small G proteins have key roles in signal transduction pathways. They are switched from the signaling 'on' to the non-signaling 'off' state when GTPase-activating proteins (GAPs) provide a catalytic residue. The ancient signal recognition particle (SRP)-type GTPases form GTP-dependent homo- and heterodimers and deviate from the canonical switch paradigm in that no GAPs have been identified. Here we show that the YlxH protein activates the SRP-GTPase FlhF. The crystal structure of the Bacillus subtilis FlhF-effector complex revealed that the effector does not contribute a catalytic residue but positions the catalytic machinery already present in SRP-GTPases. We provide a general concept that might also apply to the RNA-driven activation of the universally conserved, co-translational protein-targeting machinery comprising the SRP-GTPases Ffh and FtsY. Our study exemplifies the evolutionary transition from RNA- to protein-driven activation in SRP-GTPases and suggests that the current view on SRP-mediated protein targeting is incomplete.
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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.