Open Access
International Journal of Molecular Sciences, volume 23, issue 7, pages 3862
Dimerization Activity of a Disordered N-Terminal Domain from Drosophila CLAMP Protein
Tikhonova Evgeniya
1
,
Mariasina Sofia
2
,
Arkova Olga
3
,
Maksimenko Oksana
3
,
Georgiev P. G.
1
,
Бончук А. Н.
1, 3
Publication type: Journal Article
Publication date: 2022-03-31
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 5.6
ISSN: 16616596, 14220067
PubMed ID:
35409222
Catalysis
Organic Chemistry
Inorganic Chemistry
Physical and Theoretical Chemistry
Computer Science Applications
Spectroscopy
Molecular Biology
General Medicine
Abstract
In Drosophila melanogaster, CLAMP is an essential zinc-finger transcription factor that is involved in chromosome architecture and functions as an adaptor for the dosage compensation complex. Most of the known Drosophila architectural proteins have structural N-terminal homodimerization domains that facilitate distance interactions. Because CLAMP performs architectural functions, we tested its N-terminal region for the presence of a homodimerization domain. We used a yeast two-hybrid assay and biochemical studies to demonstrate that the adjacent N-terminal region between 46 and 86 amino acids is capable of forming homodimers. This region is conserved in CLAMP orthologs from most insects, except Hymenopterans. Biophysical techniques, including nuclear magnetic resonance (NMR) and small-angle X-ray scattering (SAXS), suggested that this domain lacks secondary structure and has features of intrinsically disordered regions despite the fact that the protein structure prediction algorithms suggested the presence of beta-sheets. The dimerization domain is essential for CLAMP functions in vivo because its deletion results in lethality. Thus, CLAMP is the second architectural protein after CTCF that contains an unstructured N-terminal dimerization domain.
Citations by journals
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International Journal of Molecular Sciences
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International Journal of Molecular Sciences
3 publications, 60%
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Current Opinion in Chemical Biology
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Current Opinion in Chemical Biology
1 publication, 20%
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Citations by publishers
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Multidisciplinary Digital Publishing Institute (MDPI)
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Multidisciplinary Digital Publishing Institute (MDPI)
3 publications, 60%
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Elsevier
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Elsevier
1 publication, 20%
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- We do not take into account publications that without a DOI.
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- Statistics recalculated weekly.
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Tikhonova E. et al. Dimerization Activity of a Disordered N-Terminal Domain from Drosophila CLAMP Protein // International Journal of Molecular Sciences. 2022. Vol. 23. No. 7. p. 3862.
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Tikhonova E., Mariasina S., Arkova O., Maksimenko O., Georgiev P. G., Бончук А. Н. Dimerization Activity of a Disordered N-Terminal Domain from Drosophila CLAMP Protein // International Journal of Molecular Sciences. 2022. Vol. 23. No. 7. p. 3862.
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TY - JOUR
DO - 10.3390/ijms23073862
UR - https://doi.org/10.3390%2Fijms23073862
TI - Dimerization Activity of a Disordered N-Terminal Domain from Drosophila CLAMP Protein
T2 - International Journal of Molecular Sciences
AU - Tikhonova, Evgeniya
AU - Mariasina, Sofia
AU - Maksimenko, Oksana
AU - Arkova, Olga
AU - Georgiev, P. G.
AU - Бончук, А. Н.
PY - 2022
DA - 2022/03/31 00:00:00
PB - Multidisciplinary Digital Publishing Institute (MDPI)
SP - 3862
IS - 7
VL - 23
PMID - 35409222
SN - 1661-6596
SN - 1422-0067
ER -
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@article{2022_Tikhonova,
author = {Evgeniya Tikhonova and Sofia Mariasina and Oksana Maksimenko and Olga Arkova and P. G. Georgiev and А. Н. Бончук},
title = {Dimerization Activity of a Disordered N-Terminal Domain from Drosophila CLAMP Protein},
journal = {International Journal of Molecular Sciences},
year = {2022},
volume = {23},
publisher = {Multidisciplinary Digital Publishing Institute (MDPI)},
month = {mar},
url = {https://doi.org/10.3390%2Fijms23073862},
number = {7},
pages = {3862},
doi = {10.3390/ijms23073862}
}
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Tikhonova, Evgeniya, et al. “Dimerization Activity of a Disordered N-Terminal Domain from Drosophila CLAMP Protein.” International Journal of Molecular Sciences, vol. 23, no. 7, Mar. 2022, p. 3862. https://doi.org/10.3390%2Fijms23073862.