ArticleMolecular microbiology2017
The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]
Article in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 18 citations in OpenAlex.
- Deciphering the function of Com_YlbF domain-containing proteins inJournal of bacteriology · 2025Article
- Pleiotropic hubs drive bacterial surface competition through parallel changes in colony composition and expansion.PLoS biology · 2023Article
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- Formation of a stable RNase Y-RicT (YaaT) complex requires RicA (YmcA) and RicF (YlbF).bioRxiv : the preprint server for biology · 2023Article
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- Heme A Synthase Deficiency Affects the Ability ofInternational journal of molecular sciences · 2022Article
- Role of Glutamate Synthase in Biofilm Formation by Bacillus subtilis.Journal of bacteriology · 2020Article
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- Maturation of polycistronic mRNAs by the endoribonuclease RNase Y and its associated Y-complex inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- ClpC and MecA, components of a proteolytic machine, prevent Spo0A-P-dependent transcription without degradation.Molecular microbiology · 2018Article
- Protein lysine acetylation plays a regulatory role in Bacillus subtilis multicellularity.PloS one · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
During times of environmental insult, Bacillus subtilis undergoes developmental changes leading to biofilm formation, sporulation and competence. Each of these states is regulated in part by the phosphorylated form of the master response regulator Spo0A (Spo0A∼P). The phosphorylation state of Spo0A is controlled by a multi-component phosphorelay. RicA, RicF and RicT (previously YmcA, YlbF and YaaT) have been shown to be important regulatory proteins for multiple developmental fates. These proteins directly interact and form a stable complex, which has been proposed to accelerate the phosphorelay. Indeed, this complex is sufficient to stimulate the rate of phosphotransfer amongst the phosphorelay proteins in vitro. In this study, we demonstrate that two [4Fe-4S]
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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.