The Conserved Glutamine-rich Region of Chick Csal1 and Csal3 Mediates Protein Interactions with Other Spalt Family Members
Open accessAbstract
Members of the spalt family of zinc finger-containing proteins have been implicated in development and disease. However, very little is known about the molecular function of spalt proteins. We have used biochemical approaches to characterize functional domains of two chick spalt homologs, csal1 and csal3. We show that csal1 and csal3 proteins repress transcription and that they can interact with each other. Furthermore, we found that truncated chick spalt proteins, similar to the truncated spalt protein expressed in the human congenital disorder Townes-Brocks syndrome, affect the nuclear localization of full-length spalt. Our findings have implications for the understanding of Townes-Brocks syndrome and the role of spalt genes in normal development. We propose that truncated spalt can exert a dominant negative effect and is able to interfere with the correct function of full-length protein, by causing its displacement from the nucleus. This could affect the transcriptional repressor activity of spalt and DNA binding. Spalt protein truncations could also affect the function of other spalt family members in various tissues.
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The Q-rich sequence is comparatively depleted of population missense mutations (VdVp = 0.50).
“Three regions were observed to be comparatively depleted of population missense mutations: the N-terminal NuRD binding motif (Lauberth & Rauchman, 2006) (VdVp = 0.22); a glutamine-rich (Q-rich) sequence that has been reported to participate in SALL protein homo- and heterodimer formation (VdVp = 0.50) (Sweetman et al, 2003); and ZFC4, which is essential for SALL4 function in mice (VdVp = 0.47) (P”
From Structure of SALL4 zinc finger domain reveals link between AT-rich DNA binding and Okihiro syndrome (2023) · cites this paper as Sweetman et al, 2003
The minimal SALL4 multimerisation domain mapped here is longer than the 22 amino acids Q-rich region previously proposed to form the interaction domain.
“The minimal SALL4 multimerisation domain mapped here is longer than the 22 amino acids Q-rich region previously proposed to form the interaction domain 31 .”
From Tetramerisation governs SALL transcription factor function in development and disease (2025) · cites this paper as [31]
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References 31 · Cited by 63
- Authors
- Sweetman, D., Smith, T., Farrell, E. R., Chantry, A., & Münsterberg, A.
- Affiliations
- University of East Anglia (GB)
- University of Dundee (GB)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-02
- Volume
- 278
- Issue
- 8
- Pages
- 6560-6566
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2002566405
- Cited by
- 63
- References
- 31
- Citations by year
- 2025: 4 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 3 · 2019: 1 · 2018: 3 · 2017: 1 · 2016: 3 · 2015: 1 · 2014: 3 · 2013: 1 · 2012: 1
- FWCI
- 1.95
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ORCA Online Research @Cardiff (Cardiff University) (submittedVersion)
- UEA Digital Repository (University of East Anglia) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
- Keywords
- glutamine-rich region, zinc finger proteins, transcriptional repression, protein-protein interaction, Townes-Brocks syndrome, dominant negative effect, nuclear localization, chick embryo development
- MeSH terms
- Amino Acid Sequence, Animals, Cell Line, Chick Embryo, Disease Models, Animal, Extremities, Glutamine, Humans, Molecular Sequence Data, Morphogenesis, Peptide Fragments, Recombinant Proteins, Syndrome, Transcription Factors, Transfection, Zinc Fingers, Conserved Sequence, Homeodomain Proteins, Protein Isoforms, Xenopus Proteins
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