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The potent PHL4 transcription factor effector domain contains significant disorder
Open accessPublished version of a preprint
Abstract
The phosphate‐starvation response transcription‐factor protein family is essential to plant response to low‐levels of phosphate. Proteins in this transcription factor (TF) family act by altering various gene expression levels, such as increasing levels of the acid phosphatase proteins which catalyze the conversion of inorganic phosphates to bio‐available compounds. There are few structural characterizations of proteins in this TF family, none of which address the potent TF activation domains. The phosphate‐starvation response‐like protein‐4 (PHL4) protein from this family has garnered interest due to the unusually high TF activation activity of the N‐terminal domain. Here, we demonstrate using solution nuclear magnetic resonance (NMR) measurements that the PHL4 N‐terminal activating TF effector domain is mainly an intrinsically disordered domain of over 200 residues, and that the C‐terminal region of PHL4 is also disordered. Additionally, we present evidence from size‐exclusion chromatography, diffusion NMR measurements, and a cross‐linking assay suggesting full‐length PHL4 forms a trimeric or tetrameric assembly. Together, the data indicate the N‐ and C‐terminal disordered domains in PHL4 flank a central folded region that likely forms the ordered oligomer of PHL4. This work provides a foundation for future studies detailing how the conformations and molecular motions of PHL4 change as it acts as a potent activator of gene expression in phosphate metabolism. Such a detailed mechanistic understanding of TF function will benefit genetic engineering efforts that take advantage of this activity to boost transcriptional activation of genes across different organisms.
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Research works printed but not linked: 1
- 10.1021/jp013403 · DOI
Metadata
- Authors
- Fonda, B. D., & Murray, D. T.
- Affiliations
- University of California, Davis (US)
- University of Connecticut (US)
- Corresponding author
- Murray, Dylan T.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2024-11-16
- Volume
- 33
- Issue
- 12
- Pages
- e5214-e5214
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- PMC
- PMC11568365
- OpenAlex
- W4404432748
- Cited by
- 1
- References
- 55
- Citations by year
- 2026: 1
- FWCI
- 0.14
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Protein Science (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed Central (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-sa)
- Funders
- University of California, Davis
- National Science Foundation (DBI‐0722538)
- National Institutes of Health (S10RR013871‐01A1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant nutrient uptake and metabolism
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- intrinsically disordered regions, transactivation domain, protein oligomerization, phosphate metabolism, acid phosphatase, gene expression regulation, protein conformational dynamics
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