Halogenation of tyrosine perturbs large-scale protein self-organization.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
17 08 2022
17 08 2022
Historique:
received:
08
03
2022
accepted:
04
08
2022
entrez:
17
8
2022
pubmed:
18
8
2022
medline:
20
8
2022
Statut:
epublish
Résumé
Protein halogenation is a common non-enzymatic post-translational modification contributing to aging, oxidative stress-related diseases and cancer. Here, we report a genetically encodable halogenation of tyrosine residues in a reconstituted prokaryotic filamentous cell-division protein (FtsZ) as a platform to elucidate the implications of halogenation that can be extrapolated to living systems of much higher complexity. We show how single halogenations can fine-tune protein structures and dynamics of FtsZ with subtle perturbations collectively amplified by the process of FtsZ self-organization. Based on experiments and theories, we have gained valuable insights into the mechanism of halogen influence. The bending of FtsZ structures occurs by affecting surface charges and internal domain distances and is reflected in the decline of GTPase activities by reducing GTP binding energy during polymerization. Our results point to a better understanding of the physiological and pathological effects of protein halogenation and may contribute to the development of potential diagnostic tools.
Identifiants
pubmed: 35977922
doi: 10.1038/s41467-022-32535-2
pii: 10.1038/s41467-022-32535-2
pmc: PMC9385671
doi:
Substances chimiques
Bacterial Proteins
0
Cytoskeletal Proteins
0
Tyrosine
42HK56048U
Guanosine Triphosphate
86-01-1
Banques de données
figshare
['10.6084/m9.figshare.20368626.v1']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4843Informations de copyright
© 2022. The Author(s).
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