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An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (RNA-seq)

ABSTRACT: An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (RNA-seq)

PROVIDER: PRJNA644363 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12157778.fastq.gz	Fastqsanger.gz
	SRR12157779.fastq.gz	Fastqsanger.gz
	SRR12157780.fastq.gz	Fastqsanger.gz
	SRR12157781.fastq.gz	Fastqsanger.gz

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An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation

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An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (Tn-seq)

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An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (Tn-seq)

Project description:How cellular checkpoints couple the orderly assembly of macromolecular machines with cell cycle progression is poorly understood. The alpha-proteobacterium Caulobacter crescentus assembles a single polar flagellum during each cell cycle. We discovered that expression of multiple flagellin transcripts is licensed by a translational checkpoint responsive to a dual input signal: a secretion-competent hook-basal-body (HBB) structure and a surge in the FlaF secretion chaperone during cytokinesis, instructed by the cell cycle circuitry. We find that the unorthodox FljJ flagellin, one of six flagellin paralogs, acts as checkpoint linchpin, binding both FlaF and the FlbT translational regulator. FljJ recruits FlbT to inhibit translation at the 5’ untranslated region in other flagellin transcripts before HBB assembly. Once FlaF is synthesized and stabilized, it directs FljJ secretion through the HBB, thereby separating FlbT from its co-activator and relieving translational inhibition. The FlbT/FlaF pair is wide-spread and functional properties are conserved in alpha-proteobacteria, including pathogens.

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An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation (RNA-seq)

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An unorthodox flagellin paralog integrates cell cycle and flagellar assembly cues for flagellin translation

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2020-10-27 | GSE153955 | GEO

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Elucidation of the glycan structure of the b-type flagellin of Pseudomonas aeruginosa PAO1

Project description:Flagella are essential for motility and pathogenicity in many bacteria. The main component of the flagellar filament, flagellin, often undergoes post-translational modifications, with glycosylation being a common occurrence. In Pseudomonas aeruginosa PAO1, the b-type flagellin is O-glycosylated with a structure that, in addition to an unknown moiety, is known to include a rhamnose and a phospho-group. This resembles a well-characterized glycan (Type A) in Clostridioides difficile strain 630, which features an N-acetylglucosamine linked to an N-methylthreonine via a phosphodiester bond. This study aimed to characterize the b-type glycan structure in Pseudomonas aeruginosa PAO1 using a set of mass spectrometry experiments. For this purpose, we used wild-type P. aeruginosa PAO1 and several gene mutants from the b-type glycan biosynthetic cluster. Moreover, we compared the mass spectrometry characteristics of the b-type glycan with those of in vitro modified Type A-peptides from C. difficile strain 630. Our results demonstrate that the thus far unknown moiety of the b-type glycan in P. aeruginosa consists of an N,N-dimethylthreonine. These data allowed us to refine our model of the flagellin glycan biosynthetic pathway in both P. aeruginosa PAO1 and C. difficile strain 630.

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