ArticleProceedings of the National Academy of Sciences of the United States of America2016
Phosphorylation of spore coat proteins by a family of atypical protein kinases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 67 citations in OpenAlex.
- Uncovering enzymatic tools promoting lignocellulose breakdown in the anaerobic bacterium Ruminiclostridium cellulolyticum.Communications biology · 2025Article
- Targeted protein evolution in the gut microbiome by diversity-generating retroelements.Science (New York, N.Y.) · 2025Article
- Review
- Surface Display Technologies for Whole-Cell Biocatalysts: Advances in Optimization Strategies, Food Applications, and Future Perspectives.Foods (Basel, Switzerland) · 2025Review
- Recent progress in proteins regulating the germination ofJournal of bacteriology · 2025Review
- Targeted protein evolution in the gut microbiome by diversity-generating retroelements.bioRxiv : the preprint server for biology · 2024Article
- Molecular mechanisms that govern infection and antifungal resistance in Mucorales.Microbiology and molecular biology reviews : MMBR · 2024Review
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Review
- Article
- Mucormycosis in 2023: an update on pathogenesis and management.Frontiers in cellular and infection microbiology · 2023Review
- Article
- CotG controls spore surface formation in response to the temperature of growth in Bacillus subtilis.Environmental microbiology · 2022Article
- Identification of selenoprotein O substrates using a biotinylated ATP analog.Methods in enzymology · 2022Article
- Methods for discovering catalytic activities for pseudokinases.Methods in enzymology · 2022Article
- In silico prediction and structure-based multitargeted molecular docking analysis of selected bioactive compounds against mucormycosis.Bulletin of the National Research Centre · 2022Article
- Co‑cultivation of the anaerobic fungus Caecomyces churrovis with Methanobacterium bryantii enhances transcription of carbohydrate binding modules, dockerins, and pyruvate formate lyases on specific substrates.Biotechnology for biofuels · 2021Article
- Phenogenomic Characterization of a Newly Domesticated and Novel Species from the GenusApplied and environmental microbiology · 2021Article
- Article
- Host-Pathogen Molecular Factors Contribute to the Pathogenesis ofCurrent tropical medicine reports · 2021Review
Corrections and comments
- Commented on by
- Comment on
Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
The modification of proteins by phosphorylation occurs in all life forms and is catalyzed by a large superfamily of enzymes known as protein kinases. We recently discovered a family of secretory pathway kinases that phosphorylate extracellular proteins. One member, family with sequence similarity 20C (Fam20C), is the physiological Golgi casein kinase. While examining distantly related protein sequences, we observed low levels of identity between the spore coat protein H (CotH), and the Fam20C-related secretory pathway kinases. CotH is a component of the spore in many bacterial and eukaryotic species, and is required for efficient germination of spores in Bacillus subtilis; however, the mechanism by which CotH affects germination is unclear. Here, we show that CotH is a protein kinase. The crystal structure of CotH reveals an atypical protein kinase-like fold with a unique mode of ATP binding. Examination of the genes neighboring cotH in B. subtilis led us to identify two spore coat proteins, CotB and CotG, as CotH substrates. Furthermore, we show that CotH-dependent phosphorylation of CotB and CotG is required for the efficient germination of B. subtilis spores. Collectively, our results define a family of atypical protein kinases and reveal an unexpected role for protein phosphorylation in spore biology.
Indexed as
Identifiers
What OpenQuestion holds
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.