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The motility defect caused by absence of the transcriptional regulator LdtR in Sinorhizobium meliloti is restored by mutations in the motility genes motA and motS

ABSTRACT: The motility defect caused by absence of the transcriptional regulator LdtR in Sinorhizobium meliloti is restored by mutations in the motility genes motA and motS

PROVIDER: PRJNA1055534 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27321275.fastq.gz	Fastqsanger.gz
	SRR27321276.fastq.gz	Fastqsanger.gz
	SRR27321277.fastq.gz	Fastqsanger.gz
	SRR27321278.fastq.gz	Fastqsanger.gz
	SRR27321279.fastq.gz	Fastqsanger.gz

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The motility defect caused by absence of the transcriptional regulator LdtR in Sinorhizobium meliloti is restored by mutations in the motility genes motA and motS

Project description:The flagellar motor is a powerful macromolecular machine used to propel bacteria through various environments. Flagellar motility of the alpha-proteobacterium Sinorhizobium meliloti is nearly abolished in the absence of the transcriptional regulator LdtR, which is involved in peptidoglycan remodeling. We report that LdtR does not regulate motility gene transcription. Remarkably, the motility defects of the DldtR mutant can be restored by secondary mutations in the motility gene motA or a previously uncharacterized gene in the flagellar regulon, which we named motS. MotS is not essential for S. meliloti motility and may serve an accessory role in flagellar motor function. Structural modeling predicts that MotS is comprised of an N-terminal transmembrane segment, a long-disordered region, and a conserved β-sandwich domain. The C-terminus of MotS is localized in the periplasm. Genetics-based substitution of MotA with a MotAG12S variant protein also restored the ΔldtR motility defect. The MotAG12S variant causes a local polarity shift at the periphery of the MotAB stator units. We propose that MotS may be required for optimal alignment of stators in wild-type flagellar motors but becomes detrimental in cells with altered peptidoglycan. Similarly, the polarity shift in the stator units composed of MotB/MotAG12S might stabilize its interaction with altered peptidoglycan.

2024-06-18 | GSE251837 | GEO

MOTS-c peptide binding protein

Project description:To elucidate the molecular mechanism of MOTS-c against NASH progression, we screened for potential MOTS-c binding proteins using biotin-labeled MOTS-c and HuProt human proteome microarray.

2024-01-18 | GSE253264 | GEO

Effect of MOTS-c treatment on cast immobilization-induced skeletal muscle atrophy

Project description:To understand the effect of MOTS-c treatment on cast immobilization-induced skeletal muscle atrophy, we injected MOTS-c into casted mice. We then performed gene expression profiling analysis using data obtained from RNA-seq of three groups: non-immobilization group, immobilization control group, and immobilization and MOTS-c treated group.

2024-07-03 | GSE212709 | GEO

The mitochondrial-encoded MOTS-c prevents pancreatic islet destruction in autoimmune diabetes

Project description:Mitochondria are principal metabolic organelles that are increasingly unveiled as immune regulators. However, it is currently not known whether mitochondrial-encoded peptides modulate T cells to induce changes in phenotype and function. Here, we found that MOTS-c prevented autoimmune β-cell destruction via phenotypical and functional changes of T cells in NOD mice, a type 1 diabetes (T1D) animal model. MOTS-c ameliorated the development of hyperglycemia and reduced islet-infiltrating immune cells. Furthermore, adoptive transfer of T cells from MOTS-c-treated NOD mice significantly decreased the incidence of diabetes in NOD-SCID mice. Metabolic and genomic analysis revealed that MOTS-c modulated T cell phenotype and function by regulating TCR/mTORC1 pathway. We observed that T1D patients had a lower serum MOTS-c level than healthy controls. Furthermore, MOTS-c reduced T cell activation by alleviating T cells from the glycolytic stress in T1D patients suggesting a potential therapeutic implication. Our findings indicate that the MOTS-c acts as a regulator of T cell phenotype and function in autoimmune diabetes.

2021-03-06 | GSE168324 | GEO

Effect of K14Q MOTS-c treatment on cast immobilization-induced skeletal muscle atrophy

Project description:To understand the effect of K14Q MOTS-c treatment on cast immobilization-induced skeletal muscle atrophy, we injected K14Q MOTS-c into casted mice.

2025-08-15 | GSE274924 | GEO

Mitochondrial-encoded peptide MOTS-c prevents pancreatic islet cell senescence to delay diabetes

Project description:To understand the mechanism underlying the role of MOTS-c in protecting pancreatic islets from senescence, we performed gene microarray analyses in pancreatic islet cells treated with either MOTS-c or a scrambled peptide

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MOTS-c peptide binding protein

Project description:MOTS-c peptide binding protein

| PRJNA1064922 | ENA

MOTS-c: A Novel Peptide Encoded by a Short Mitochondrial Open Reading Frame Regulates Metabolic Homeostasis

Project description:Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The recent identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of additional sORFs in the mtDNA that yield bioactive peptides. Here we report the identification of a sORF within the mitochondrial 12S rRNA encoding a 16-amino-acid peptide named MOTS-c (mitochondrial open-reading-frame of the twelve S rRNA -c) that regulates insulin sensitivity and metabolic homeostasis. MOTS-c is detected in various tissues and in circulation in an age-dependent manner. Its primary target organ appears to be the skeletal muscle and its cellular actions inhibit the folate cycle and its tethered de novo purine biosynthesis, causing a significant accumulation of AICAR levels concomitantly with AMPK activation. MOTS-c treatment in mice prevented age-dependent and high-fat diet-induced insulin resistance, as well as diet-induced obesity. These results suggest that mitochondria may be more actively engaged in regulating metabolic homeostasis than previously recognized, through the production of peptides encoded within its genome that act at the cellular and organismal level. Human embryonic kidney cells (HEK293 cell line) were cultured in 10-cm dishes in 7 mL of phenol-free DMEM supplemented with 10% FBS and incubated with water (controls) or the 16-amino-acid peptide mitochondrial open-reading-frame of the twelve S rRNA-c (MOTS-c, 10 uM) for 4 or 72 hours prior to RNA extraction.

2015-03-07 | E-GEOD-65068 | biostudies-arrayexpress

MKL1 deficiency results in a severe neutrophil motility defect due to impaired actin polymerization

Project description:MKL1 deficiency results in a severe neutrophil motility defect due to impaired actin polymerization

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Energy metabolism and cell motility defect in NK-cells from patients with Hepatocellular Carcinoma

Project description:Energy metabolism and cell motility defect in NK-cells from patients with Hepatocellular Carcinoma

| PRJNA528645 | ENA