A poly-histidine motif of HOXA1 is involved in regulatory interactions with cysteine-rich proteins
(2024) Biochimica et Biophysica Acta. Gene Regulatory Mechanisms — Vol. 1867, n° 1, p. 194993 (2024)
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- Homopolymeric amino acid repeats are found in about 24 % of human proteins and are over-represented in transcriptions factors and kinases. Although relatively rare, homopolymeric histidine repeats (polyH) are more significantly found in proteins involved in the regulation of embryonic development. To gain a better understanding of the role of polyH in these proteins, we used a bioinformatic approach to search for shared features in the interactomes of polyH-containing proteins in human. Our analysis revealed that polyH protein interactomes are enriched in cysteine-rich proteins and in proteins containing (a) cysteine repeat(s). Focusing on HOXA1, a HOX transcription factor displaying one long polyH motif, we identified that the polyH motif is required for the HOXA1 interaction with such cysteine-rich proteins. We observed a correlation between the length of the polyH repeat and the strength of the HOXA1 interaction with one Cys-rich protein, MDFI. We also found that metal ion chelators disrupt the HOXA1-MDFI interaction supporting that such metal ions are required for the interaction. Furthermore, we identified three polyH interactors which down-regulate the transcriptional activity of HOXA1. Taken together, our data point towards the involvement of polyH and cysteines in regulatory interactions between proteins, notably transcription factors like HOXA1.
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Marchese, D., Guislain, F., Pringels, T., Bridoux, L., & Rezsohazy, R. (2024). A poly-histidine motif of HOXA1 is involved in regulatory interactions with cysteine-rich proteins. Biochimica et Biophysica Acta. Gene Regulatory Mechanisms, 1867(1), 194993. https://doi.org/10.1016/j.bbagrm.2023.194993 (Original work published 2024)