<div class="csl-bib-body">
<div class="csl-entry">Soydan, M., & Conibear, A. C. (2024, December 5). <i>Site-specific acetylation of HMGN1 within the nucleosome binding domain</i> [Poster Presentation]. 13th Austrian Peptide Symposium, Wien, Austria.</div>
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dc.identifier.uri
http://hdl.handle.net/20.500.12708/206406
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dc.description.abstract
Site-specific acetylation of HMGN1 within the nucleosome binding domain
Medine Soydan, and Anne C. Conibear
Institute of Applied Synthetic Chemistry, Faculty of Technical Chemistry, TU Wien, Vienna, Austria
Email: medine.soydan@tuwien.ac.at
Chromatin is a complex of RNA, DNA, and proteins to store the genome of eukaryotes in physiological conditions and to organize DNA metabolic pathways. DNA replication, transcription, recombination, and chromosome segregation are the major biological processes that chromatin is involved in. Nucleosomes are the repeating units in chromatin structure, and can undergo certain modifications. Several regulatory proteins, including non-histone proteins like HMGN1, can participate in chromatin structure modification and may result in functional change. HMGN1 is subjected intensely to posttranslational modifications (PTMs), mainly lysine acetylation and serine phosphorylation. Although various biological functions are attributed to HMGN1 and its PTMs, the precise effects of its PTMs on the biological function remain largely unknown. We aim to investigate the effects of lysine acetylation in the nucleosome binding domain of HMGN1 on interactions of HMGN1 with nucleosomes. We present the synthesis of site-specifically acetylated HMGN1 variants by a semi-synthetic approach. We performed structural analysis of the site-specifically acetylated HMGN1 variants by CD spectroscopy, which shows that both unmodified and acetylated variants of HMGN1 are intrinsically disordered, as reported in the literature. We also conducted preliminary thermal stability shift assays to examine the interactions of HMGN1 variants with nucleosomes. We anticipate the assays will provide more insights on how HMGN1 accomplishes specific functions within the cells due to PTMs at precise positions.
en
dc.description.sponsorship
FWF - Österr. Wissenschaftsfonds
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dc.language.iso
en
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dc.subject
Peptide chemistry
en
dc.subject
Acetylation
en
dc.subject
nucleosome binding
en
dc.title
Site-specific acetylation of HMGN1 within the nucleosome binding domain
en
dc.type
Presentation
en
dc.type
Vortrag
de
dc.relation.grantno
P 36101-B
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dc.type.category
Poster Presentation
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tuw.project.title
Posttranslationale Modifikation von HMGN1 in DNA-Verpackung
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tuw.researchTopic.id
M6
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tuw.researchTopic.name
Biological and Bioactive Materials
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tuw.researchTopic.value
100
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tuw.publication.orgunit
E163-03-2 - Forschungsgruppe Molekulare Chemie und Chemische Biologie
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tuw.author.orcid
0009-0008-5198-0025
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tuw.author.orcid
0000-0002-5482-6225
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tuw.event.name
13th Austrian Peptide Symposium
en
tuw.event.startdate
05-12-2024
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tuw.event.enddate
05-12-2024
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tuw.event.online
On Site
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tuw.event.type
Event for scientific audience
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tuw.event.place
Wien
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tuw.event.country
AT
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tuw.event.institution
Austrian Peptide Community under the auspices of the European Peptide Society
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tuw.event.presenter
Soydan, Medine
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tuw.event.track
Single Track
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wb.sciencebranch
Chemie
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wb.sciencebranch
Chemische Verfahrenstechnik
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wb.sciencebranch
Pharmazie, Pharmakologie, Toxikologie
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wb.sciencebranch.oefos
1040
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wb.sciencebranch.oefos
2040
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wb.sciencebranch.oefos
3012
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wb.sciencebranch.value
60
-
wb.sciencebranch.value
20
-
wb.sciencebranch.value
20
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item.languageiso639-1
en
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item.openairetype
conference poster not in proceedings
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item.grantfulltext
restricted
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item.fulltext
no Fulltext
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item.cerifentitytype
Publications
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item.openairecristype
http://purl.org/coar/resource_type/c_18co
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crisitem.author.dept
E163-03-2 - Forschungsgruppe Molekulare Chemie und Chemische Biologie
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crisitem.author.dept
E163-03-2 - Forschungsgruppe Molekulare Chemie und Chemische Biologie
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crisitem.author.orcid
0009-0008-5198-0025
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crisitem.author.orcid
0000-0002-5482-6225
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crisitem.author.parentorg
E163-03 - Forschungsbereich Organische und Biologische Chemie
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crisitem.author.parentorg
E163-03 - Forschungsbereich Organische und Biologische Chemie
