ArticleProceedings of the National Academy of Sciences of the United States of America2009
Functional equivalence of HMGA- and histone H1-like domains in a bacterial transcriptional factor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- House of CarDs: Functional insights into the transcriptional regulator CdnL.Molecular microbiology · 2024Review
- Coenzyme BEnvironmental microbiology · 2022Article
- Light-Triggered Carotenogenesis inMicroorganisms · 2021Review
- 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
- Phylogeny-Based Systematization of Arabidopsis Proteins with Histone H1 Globular Domain.Plant physiology · 2017Article
- Caulobacter crescentus CdnL is a non-essential RNA polymerase-binding protein whose depletion impairs normal growth and rRNA transcription.Scientific reports · 2017Article
- Article
- Structural insights into RNA polymerase recognition and essential function of Myxococcus xanthus CdnL.PloS one · 2014Article
- High-mobility-group a-like CarD binds to a DNA site optimized for affinity and position and to RNA polymerase to regulate a light-inducible promoter in Myxococcus xanthus.Journal of bacteriology · 2013Article
- 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.Nucleic acids research · 2010Article
- Myxobacteria, polarity, and multicellular morphogenesis.Cold Spring Harbor perspectives in biology · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Histone H1 and high-mobility group A (HMGA) proteins compete dynamically to modulate chromatin structure and regulate DNA transactions in eukaryotes. In prokaryotes, HMGA-like domains are known only in Myxococcus xanthus CarD and its Stigmatella aurantiaca ortholog. These have an N-terminal module absent in HMGA that interacts with CarG (a zinc-associated factor that does not bind DNA) to form a stable complex essential in regulating multicellular development, light-induced carotenogenesis, and other cellular processes. An analogous pair, CarD(Ad) and CarG(Ad), exists in another myxobacterium, Anaeromyxobacter dehalogenans. Intriguingly, the CarD(Ad) C terminus lacks the hallmark HMGA DNA-binding AT-hooks and instead resembles the C-terminal region (CTR) of histone H1. We find that CarD(Ad) alone could not replace CarD in M. xanthus. By contrast, when introduced with CarG(Ad), CarD(Ad) functionally replaced CarD in regulating not just 1 but 3 distinct processes in M. xanthus, despite the lower DNA-binding affinity of CarD(Ad) versus CarD in vitro. The ability of the cognate CarD(Ad)-CarG(Ad) pair to interact, but not the noncognate CarD(Ad)-CarG, rationalizes these data. Thus, in chimeras that conserve CarD-CarG interactions, the H1-like CTR of CarD(Ad) could replace the CarD HMGA AT-hooks with no loss of function in vivo. More tellingly, even chimeras with the CarD AT-hook region substituted by human histone H1 CTR or full-length H1 functioned in M. xanthus. Our domain-swap analyses showing functional equivalence of HMGA AT-hooks and H1 CTR in prokaryotic transcriptional regulation provide molecular insights into possible modes of action underlying their biological roles.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.