ArticleMicrobes and environments2019
An Aggregation-defective Mutant of Methanothermobacter sp. CaT2 Reveals Unique Protein-dependent Aggregation.
Article in Microbes and environments, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 12 citations in OpenAlex.
- A global survey of intramolecular isopeptide bonds.Protein science : a publication of the Protein Society · 2025Article
- Proteomic and metabolomic profiling of extracellular vesicles produced by human gut archaea.Nature communications · 2025Article
- Biofilm lifestyle across different lineages of ammonia-oxidizing archaea.The ISME journal · 2025Article
- Methanogenic partner influences cell aggregation and signalling of Syntrophobacterium fumaroxidans.Applied microbiology and biotechnology · 2024Article
- Mechanisms of microbial co-aggregation in mixed anaerobic cultures.Applied microbiology and biotechnology · 2024Review
- Phenotypic and genomic characterization ofApplied and environmental microbiology · 2024Article
- Recent Biofilm Studies Open a New Door in Microbial Ecology.Microbes and environments · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
The thermophilic hydrogenotrophic methanogen, Methanothermobacter sp. CaT2, which possesses an extracellular sugar layer, commonly aggregates by itself or with other microorganisms. To elucidate the molecular mechanisms responsible for this aggregation, the aggregation-defective mutant, CLA160, was isolated. Optical and electron microscopy observations revealed that the mutant exhibited a significant reduction in aggregation. Genomic sequencing showed that CLA160 has a single point mutation, causing a nonsense mutation in MTCT_1020, which encodes a hypothetical protein. Motif and domain analyses indicated that the hypothetical protein bears two membrane-spanning segments at the N- and C-terminal regions and a large middle repeat-containing region. The results of a bioinformatic analysis suggested that the first middle region (RII) of the protein or the whole structure is responsible for the function of the product of MTCT_1020 in the aggregation of CaT2. A treatment with proteinase K suppressed sedimentation in CaT2, indicating a reduction in aggregation, with almost no effect on sedimentation in CLA160. The addition of Ca
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