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A dual-function RNA balances carbon uptake and central metabolism in Vibrio cholerae.


ABSTRACT: Bacterial small RNAs (sRNAs) are well known to modulate gene expression by base pairing with trans-encoded transcripts and are typically non-coding. However, several sRNAs have been reported to also contain an open reading frame and thus are considered dual-function RNAs. In this study, we discovered a dual-function RNA from Vibrio cholerae, called VcdRP, harboring a 29 amino acid small protein (VcdP), as well as a base-pairing sequence. Using a forward genetic screen, we identified VcdRP as a repressor of cholera toxin production and link this phenotype to the inhibition of carbon transport by the base-pairing segment of the regulator. By contrast, we demonstrate that the VcdP small protein acts downstream of carbon transport by binding to citrate synthase (GltA), the first enzyme of the citric acid cycle. Interaction of VcdP with GltA results in increased enzyme activity and together VcdR and VcdP reroute carbon metabolism. We further show that transcription of vcdRP is repressed by CRP allowing us to provide a model in which VcdRP employs two different molecular mechanisms to synchronize central metabolism in V. cholerae.

SUBMITTER: Venkat K 

PROVIDER: S-EPMC8672173 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature

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A dual-function RNA balances carbon uptake and central metabolism in Vibrio cholerae.

Venkat Kavyaa K   Hoyos Mona M   Haycocks James Rj JR   Cassidy Liam L   Engelmann Beatrice B   Rolle-Kampczyk Ulrike U   von Bergen Martin M   Tholey Andreas A   Grainger David C DC   Papenfort Kai K  

The EMBO journal 20211006 24


Bacterial small RNAs (sRNAs) are well known to modulate gene expression by base pairing with trans-encoded transcripts and are typically non-coding. However, several sRNAs have been reported to also contain an open reading frame and thus are considered dual-function RNAs. In this study, we discovered a dual-function RNA from Vibrio cholerae, called VcdRP, harboring a 29 amino acid small protein (VcdP), as well as a base-pairing sequence. Using a forward genetic screen, we identified VcdRP as a r  ...[more]

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