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Amia ocellicauda

ABSTRACT: Amia ocellicauda overview

PROVIDER: PRJNA291112 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
		Other
	SRR12068800.fastq.gz	Fastqsanger.gz
	SRR12068801.fastq.gz	Fastqsanger.gz
	SRR12068802.fastq.gz	Fastqsanger.gz
	SRR12068803.fastq.gz	Fastqsanger.gz

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Peptide Ligands of AmiA, AliA, and AliB Proteins Determine Pneumococcal Phenotype.

Project description:The Ami-AliA/AliB oligopeptide permease of Streptococcus pneumoniae has been suggested to play a role in environmental sensing and colonisation of the nasopharynx by this human bacterial pathogen by binding peptides derived from bacterial neighbours of other species in the microbiota. Here, we investigated the effects of the peptide ligands of the permease's substrate binding proteins AmiA, AliA, and AliB on pneumococcal phenotype. AmiA and AliA ligands reduced pneumococcal growth, increased biofilm production and reduced capsule size. In contrast, AliB ligand increased growth and greatly increased bacterial chain length. A decrease in transformation rate was observed in response to all three peptides. Changes in protein expression were also observed, particularly those associated with metabolism and cell wall synthesis. Understanding interspecies bacterial communication and its effect on development of colonising versus invasive phenotypes has the potential to reveal new targets to tackle and prevent pneumococcal infections.

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amiA is a negative regulator of acetamidase expression in Mycobacterium smegmatis.

Project description:BackgroundThe acetamidase of Mycobacterium smegmatis is a highly inducible enzyme. Expression of this enzyme is increased 100-fold when the substrate acetamide is present. The acetamidase gene is found immediately downstream of three open reading frames. Two of these are proposed to be involved in regulation.ResultsWe constructed a deletion mutant in one of the upstream ORFs (amiA). This mutant (Mad1) showed a constitutively high level of acetamidase expression. We identified four promoters in the upstream region using a beta-galactosidase reporter gene. One of these (P2) was inducible in the wild-type, but was constitutively active in Mad1.ConclusionsThese results demonstrate that amiA encodes a negative regulatory protein which interacts with P2. Since amiA has homology to DNA-binding proteins, it is likely that it exerts the regulatory effect by binding to the promoter to prevent transcription.

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