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Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA

Non-histone nuclear proteins HMGB1 and HMGB2 (High Mobility Group) are involved in many biological processes, such as replication, transcription, and repair. The HMGB1 and HMGB2 proteins consist of a short N-terminal region, two DNA-binding domains, A and B, and a C-terminal sequence of glutamic and...

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Autores principales: Starkova, Tatiana Y., Polyanichko, Alexander M., Artamonova, Tatiana O., Tsimokha, Anna S., Tomilin, Alexey N., Chikhirzhina, Elena V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9962726/
https://www.ncbi.nlm.nih.gov/pubmed/36834988
http://dx.doi.org/10.3390/ijms24043577
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author Starkova, Tatiana Y.
Polyanichko, Alexander M.
Artamonova, Tatiana O.
Tsimokha, Anna S.
Tomilin, Alexey N.
Chikhirzhina, Elena V.
author_facet Starkova, Tatiana Y.
Polyanichko, Alexander M.
Artamonova, Tatiana O.
Tsimokha, Anna S.
Tomilin, Alexey N.
Chikhirzhina, Elena V.
author_sort Starkova, Tatiana Y.
collection PubMed
description Non-histone nuclear proteins HMGB1 and HMGB2 (High Mobility Group) are involved in many biological processes, such as replication, transcription, and repair. The HMGB1 and HMGB2 proteins consist of a short N-terminal region, two DNA-binding domains, A and B, and a C-terminal sequence of glutamic and aspartic acids. In this work, the structural organization of calf thymus HMGB1 and HMGB2 proteins and their complexes with DNA were studied using UV circular dichroism (CD) spectroscopy. Post-translational modifications (PTM) of HMGB1 and HMGB2 proteins were determined with MALDI mass spectrometry. We have shown that despite the similar primary structures of the HMGB1 and HMGB2 proteins, their post-translational modifications (PTMs) demonstrate quite different patterns. The HMGB1 PTMs are located predominantly in the DNA-binding A-domain and linker region connecting the A and B domains. On the contrary, HMGB2 PTMs are found mostly in the B-domain and within the linker region. It was also shown that, despite the high degree of homology between HMGB1 and HMGB2, the secondary structure of these proteins is also slightly different. We believe that the revealed structural properties might determine the difference in the functioning of the HMGB1 and HMGB2 as well as their protein partners.
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spelling pubmed-99627262023-02-26 Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA Starkova, Tatiana Y. Polyanichko, Alexander M. Artamonova, Tatiana O. Tsimokha, Anna S. Tomilin, Alexey N. Chikhirzhina, Elena V. Int J Mol Sci Article Non-histone nuclear proteins HMGB1 and HMGB2 (High Mobility Group) are involved in many biological processes, such as replication, transcription, and repair. The HMGB1 and HMGB2 proteins consist of a short N-terminal region, two DNA-binding domains, A and B, and a C-terminal sequence of glutamic and aspartic acids. In this work, the structural organization of calf thymus HMGB1 and HMGB2 proteins and their complexes with DNA were studied using UV circular dichroism (CD) spectroscopy. Post-translational modifications (PTM) of HMGB1 and HMGB2 proteins were determined with MALDI mass spectrometry. We have shown that despite the similar primary structures of the HMGB1 and HMGB2 proteins, their post-translational modifications (PTMs) demonstrate quite different patterns. The HMGB1 PTMs are located predominantly in the DNA-binding A-domain and linker region connecting the A and B domains. On the contrary, HMGB2 PTMs are found mostly in the B-domain and within the linker region. It was also shown that, despite the high degree of homology between HMGB1 and HMGB2, the secondary structure of these proteins is also slightly different. We believe that the revealed structural properties might determine the difference in the functioning of the HMGB1 and HMGB2 as well as their protein partners. MDPI 2023-02-10 /pmc/articles/PMC9962726/ /pubmed/36834988 http://dx.doi.org/10.3390/ijms24043577 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Starkova, Tatiana Y.
Polyanichko, Alexander M.
Artamonova, Tatiana O.
Tsimokha, Anna S.
Tomilin, Alexey N.
Chikhirzhina, Elena V.
Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA
title Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA
title_full Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA
title_fullStr Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA
title_full_unstemmed Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA
title_short Structural Characteristics of High-Mobility Group Proteins HMGB1 and HMGB2 and Their Interaction with DNA
title_sort structural characteristics of high-mobility group proteins hmgb1 and hmgb2 and their interaction with dna
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9962726/
https://www.ncbi.nlm.nih.gov/pubmed/36834988
http://dx.doi.org/10.3390/ijms24043577
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