Exploring the CNOT1(800–999) HEAT Domain and Its Interactions with Tristetraprolin (TTP) as Revealed by Hydrogen/Deuterium Exchange Mass Spectrometry DOI Creative Commons
Maja K. Cieplak-Rotowska, Michał Dadlez, Anna Niedźwiecka

и другие.

Biomolecules, Год журнала: 2025, Номер 15(3), С. 403 - 403

Опубликована: Март 11, 2025

CNOT1, a key scaffold in the CCR4-NOT complex, plays critical role mRNA decay, particularly regulation of inflammatory responses through its interaction with tristetraprolin. A fragment middle part CNOT1 (residues 800–999) is an example α-helical HEAT-like repeat domain. The HEAT motif evolutionarily conserved present scaffolding and transport proteins across wide range organisms. Using hydrogen/deuterium exchange mass spectrometry (HDX MS), method that has not been widely explored context repeats, we analysed structural dynamics wild-type CNOT1(800–999) two double point mutants (E893A/Y900A, E893Q/Y900H) to find individual contributions these residues molecular recognition tristetraprolin (TTP). Our results show differences interactions variants TTP peptide are due absence resulting from mutations perturbation protein structure. Nevertheless, HDX MS was able detect slight local changes induced by mutations, which usually neglected studies intermolecular interactions.

Язык: Английский

Exploring the CNOT1(800–999) HEAT Domain and Its Interactions with Tristetraprolin (TTP) as Revealed by Hydrogen/Deuterium Exchange Mass Spectrometry DOI Creative Commons
Maja K. Cieplak-Rotowska, Michał Dadlez, Anna Niedźwiecka

и другие.

Biomolecules, Год журнала: 2025, Номер 15(3), С. 403 - 403

Опубликована: Март 11, 2025

CNOT1, a key scaffold in the CCR4-NOT complex, plays critical role mRNA decay, particularly regulation of inflammatory responses through its interaction with tristetraprolin. A fragment middle part CNOT1 (residues 800–999) is an example α-helical HEAT-like repeat domain. The HEAT motif evolutionarily conserved present scaffolding and transport proteins across wide range organisms. Using hydrogen/deuterium exchange mass spectrometry (HDX MS), method that has not been widely explored context repeats, we analysed structural dynamics wild-type CNOT1(800–999) two double point mutants (E893A/Y900A, E893Q/Y900H) to find individual contributions these residues molecular recognition tristetraprolin (TTP). Our results show differences interactions variants TTP peptide are due absence resulting from mutations perturbation protein structure. Nevertheless, HDX MS was able detect slight local changes induced by mutations, which usually neglected studies intermolecular interactions.

Язык: Английский

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