The N-Terminal Region of Drosophila MSL1 Interacts with Zinc Finger Proteins and Promotes the Recruitment of the MSL Complex to the X Chromosome in Males
- 1Department of the Control of Genetic Processes, Institute of Gene Biology, Russian Academy of Sciences, 34/5 Vavilova Str., 119334 Moscow, Russia
- 2Center for Genome Research, Institute of Gene Biology, Russian Academy of Sciences, 34/5 Vavilova Str., 119334 Moscow, Russia
Abstract
The Drosophila protein male-specific lethal 1 (MSL1) is part of the five-subunit male-specific lethal (MSL) complex that binds only to the X chromosome in males. MSL1 contains a 93-amino-acid N-terminal unstructured region followed by a coiled-coil domain that forms a homodimer. The MSL1 dimer and male-specific lethal 2 (MSL2), which interacts with its coiled-coil domain, form a core that is primarily responsible for the specific recruitment of the MSL complex to X-chromosome high-affinity sites (HASs). In a yeast two-hybrid analysis, we found that the N-terminal region of MSL1, primarily amino acids 66–85 and the coiled-coil domain, interacts with many DNA-binding transcription factors. The coiled-coil domain of Drosophila virilis MSL1 (vCC) retains the ability to interact with Drosophila melanogaster MSL2 but not with zinc finger proteins. Expression of a double mutant of MSL1 (MSL1Δ20vCC), in which amino acids 66–85 (Δ20) have been deleted and the coiled-coil domain has been replaced with the vCC domain, significantly reduced dosage compensation in males due to decreased binding of the MSL complex to the X chromosome. Substitution of MSL1 with MSL1vCC in females ectopically expressing MSL2 also significantly reduced recruitment of the MSL complex to the X chromosome. Altogether, these results indicate a key role of the N-terminal region of MSL1 not only in the assembly of the MSL complex but also in its recruitment to the X chromosome in males.
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BibTeX
@article{babosha2026nterminal,
title = {{The N-Terminal Region of Drosophila MSL1 Interacts with Zinc Finger Proteins and Promotes the Recruitment of the MSL Complex to the X Chromosome in Males}},
author = {Valentin Babosha and Varvara Ryzhkova and Anastasia Revel-Muroz and Evgeniya Tikhonova and Yulia Vasileva and Oksana Maksimenko and Pavel Georgiev},
journal = {International Journal of Molecular Sciences},
year = {2026},
month = nov,
doi = {10.3390/ijms27219861},
url = {https://www.mdpi.com/1422-0067/27/21/9861},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - The N-Terminal Region of Drosophila MSL1 Interacts with Zinc Finger Proteins and Promotes the Recruitment of the MSL Complex to the X Chromosome in Males
AU - Valentin Babosha
AU - Varvara Ryzhkova
AU - Anastasia Revel-Muroz
AU - Evgeniya Tikhonova
AU - Yulia Vasileva
AU - Oksana Maksimenko
AU - Pavel Georgiev
PY - 2026
DA - 2026/11/03
JO - International Journal of Molecular Sciences
DO - 10.3390/ijms27219861
UR - https://www.mdpi.com/1422-0067/27/21/9861
AB - The Drosophila protein male-specific lethal 1 (MSL1) is part of the five-subunit male-specific lethal (MSL) complex that binds only to the X chromosome in males. MSL1 contains a 93-amino-acid N-terminal unstructured region followed by a coiled-coil domain that forms a homodimer. The MSL1 dimer and male-specific lethal 2 (MSL2), which interacts with its coiled-coil domain, form a core that is primarily responsible for the specific recruitment of the MSL complex to X-chromosome high-affinity sites (HASs). In a yeast two-hybrid analysis, we found that the N-terminal region of MSL1, primarily amino acids 66–85 and the coiled-coil domain, interacts with many DNA-binding transcription factors. The coiled-coil domain of Drosophila virilis MSL1 (vCC) retains the ability to interact with Drosophila melanogaster MSL2 but not with zinc finger proteins. Expression of a double mutant of MSL1 (MSL1Δ20vCC), in which amino acids 66–85 (Δ20) have been deleted and the coiled-coil domain has been replaced with the vCC domain, significantly reduced dosage compensation in males due to decreased binding of the MSL complex to the X chromosome. Substitution of MSL1 with MSL1vCC in females ectopically expressing MSL2 also significantly reduced recruitment of the MSL complex to the X chromosome. Altogether, these results indicate a key role of the N-terminal region of MSL1 not only in the assembly of the MSL complex but also in its recruitment to the X chromosome in males.
SN - 1422-0067
ER -