ArticleNucleic acids research2010
CdnL, a member of the large CarD-like family of bacterial proteins, is vital for Myxococcus xanthus and differs functionally from the global transcriptional regulator CarD.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 49 citations in OpenAlex.
- Ribosome engineering of Myxococcus xanthus for enhancing the heterologous production of epothilones.Microbial cell factories · 2024Article
- House of CarDs: Functional insights into the transcriptional regulator CdnL.Molecular microbiology · 2024Review
- Structural basis for regulation of a CBASS-CRISPR-Cas defense island by a transmembrane anti-σ factor and its ECF σ partner.Science advances · 2024Article
- Regulation of the transcription factor CdnL promotes adaptation to nutrient stress inPNAS nexus · 2024Article
- Regulation of the transcription factor CdnL promotes adaptation to nutrient stress inbioRxiv : the preprint server for biology · 2023Article
- Coenzyme BEnvironmental microbiology · 2022Article
- Proteomic Signatures of Microbial Adaptation to the Highest Ultraviolet-Irradiation on Earth: Lessons From a Soil Actinobacterium.Frontiers in microbiology · 2022Article
- Promoter Architecture Differences amongmSystems · 2021Article
- Light-Triggered Carotenogenesis inMicroorganisms · 2021Review
- A majority ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The conserved transcriptional regulator CdnL is required for metabolic homeostasis and morphogenesis in Caulobacter.PLoS genetics · 2020Article
- CarD contributes to diverse gene expression outcomes throughout the genome ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Ferredoxin-Like Protein FerR Regulates PrbP Activity inApplied and environmental microbiology · 2019Article
- Multifactorial control of the expression of a CRISPR-Cas system by an extracytoplasmic function σ/anti-σ pair and a global regulatory complex.Nucleic acids research · 2018Article
- LtpA, a CdnL-type CarD regulator, is important for the enzootic cycle of the Lyme disease pathogen.Emerging microbes & infections · 2018Article
- Caulobacter crescentus CdnL is a non-essential RNA polymerase-binding protein whose depletion impairs normal growth and rRNA transcription.Scientific reports · 2017Article
- Effects of Increasing the Affinity of CarD for RNA Polymerase on Mycobacterium tuberculosis Growth, rRNA Transcription, and Virulence.Journal of bacteriology · 2017Article
- Identification of the Tolfenamic Acid Binding Pocket in PrbP fromFrontiers in microbiology · 2017Article
- Mfd Protein and Transcription-Repair Coupling in Escherichia coli.Photochemistry and photobiology · 2017Review
- Mycobacterium tuberculosis Transcription Machinery: Ready To Respond to Host Attacks.Journal of bacteriology · 2016Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CarD, a global transcriptional regulator in Myxococcus xanthus, interacts with CarG via CarDNter, its N-terminal domain, and with DNA via a eukaryotic HMGA-type C-terminal domain. Genomic analysis reveals a large number of standalone proteins resembling CarDNter. These constitute, together with the RNA polymerase (RNAP) interacting domain, RID, of transcription-repair coupling factors, the CarD_TRCF protein family. We show that one such CarDNter-like protein, M. xanthus CdnL, cannot functionally substitute CarDNter (or vice versa) nor interact with CarG. Unlike CarD, CdnL is vital for growth, and lethality due to its absence is not rescued by homologs from various other bacteria. In mycobacteria, with no endogenous DksA, the function of the CdnL homolog mirrors that of Escherichia coli DksA. Our finding that CdnL, like DksA, is indispensable in M. xanthus implies that they are not functionally redundant. Cells are normal on CdnL overexpression, but divide aberrantly on CdnL depletion. CdnL localizes to the nucleoid, suggesting piggyback recruitment by factors such as RNAP, which we show interacts with CdnL, CarDNter and RID. Our study highlights a complex network of interactions involving these factors and RNAP, and points to a vital role for M. xanthus CdnL in an essential DNA transaction that affects cell division.
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