Phosphomimicking mutants: why to be careful

a 2020

Phosphomimicking mutants: why to be careful

NÁPLAVOVÁ, Alexandra, Aneta KOZELEKOVÁ a Jozef HRITZ

Základní údaje

Originální název

Phosphomimicking mutants: why to be careful

Autoři

NÁPLAVOVÁ, Alexandra, Aneta KOZELEKOVÁ a Jozef HRITZ

Vydání

XX. Workshop of Biophysical Chemists and Electrochemists, 2020

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Organizační jednotka

Středoevropský technologický institut

ISBN

978-80-210-9655-4

Klíčová slova anglicky

phosphomimicking mutant; 14-3-3; protein stability

Změněno: 5. 1. 2023 16:29, Mgr. Alexandra Náplavová

Anotace

V originále

Stability of protein is the ability to maintain its structure and thus function under stress. This stress can be caused by alternations of surroundings such as temperature or pH change, addition of denaturant, presence of salts, etc. [1]. Many methods to assess protein stability were developed, including nanoDSF, which measures changes in the intrinsic fluorescence of tryptophan during protein unfolding, to determine the melting temperature [2]. Phosphomimicking mutants are a tool commonly used to study the properties of phosphorylated proteins [3]. Here we compared thermodynamic stability of such mutant and phosphorylated form of 14-3-3ζ protein. This particular protein plays a role in regulation of many cellular functions [4]. The phosphorylation of S58 located at the dimer interface is one of the factors affecting interaction of 14-3-3ζ with its partners [5]. The results have shown, that phosphomimicking mutant S58E cannot be considered a sufficient replacement for phosphorylated 14-3-3ζ at S58. Not only does their stability differ in various conditions, with overall better stability of S58E, but their intrinsic fluorescence behaves differently as well.

Návaznosti

LM2018127, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

LTAUSA18168, projekt VaV

Název: Selektivní NMR značení jako nástroj pro charakterizaci proteinových komplexů zapojených do neurodegenerativních onemocnění

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Selektivní NMR značení jako nástroj pro charakterizaci proteinových komplexů zapojených do neurodegenerativních onemocnění, INTER-ACTION

Citovat

NÁPLAVOVÁ, Alexandra, Aneta KOZELEKOVÁ a Jozef HRITZ. Phosphomimicking mutants: why to be careful. In XX. Workshop of Biophysical Chemists and Electrochemists. 2020. ISBN 978-80-210-9655-4.

@proceedings{1688144,
   author = {Náplavová, Alexandra and Kozeleková, Aneta and Hritz, Jozef},
   booktitle = {XX. Workshop of Biophysical Chemists and Electrochemists},
   keywords = {phosphomimicking mutant; 14-3-3; protein stability},
   language = {eng},
   isbn = {978-80-210-9655-4},
   title = {Phosphomimicking mutants: why to be careful},
   url = {https://www.sci.muni.cz/labifel/files/soubory/sbornik_2020.pdf},
   year = {2020}
}

TY  - CONF
ID  - 1688144
AU  - Náplavová, Alexandra - Kozeleková, Aneta - Hritz, Jozef
PY  - 2020
TI  - Phosphomimicking mutants: why to be careful
SN  - 9788021096554
KW  - phosphomimicking mutant
KW  - 14-3-3
KW  - protein stability
UR  - https://www.sci.muni.cz/labifel/files/soubory/sbornik_2020.pdf
L2  - https://www.sci.muni.cz/labifel/files/soubory/sbornik_2020.pdf
N2  - Stability of protein is the ability to maintain its structure and thus function under stress. This stress can be caused by alternations of surroundings such as temperature or pH change, addition of denaturant, presence of salts, etc. [1]. Many methods to assess protein stability were developed, including nanoDSF, which measures changes in the intrinsic fluorescence of tryptophan during protein unfolding, to determine the melting temperature [2]. Phosphomimicking mutants are a tool commonly used to study the properties of phosphorylated proteins [3]. Here we compared thermodynamic stability of such mutant and phosphorylated form of 14-3-3ζ protein. This particular protein plays a role in regulation of many cellular functions [4]. The phosphorylation of S58 located at the dimer interface is one of the factors affecting interaction of 14-3-3ζ with its partners [5]. The results have shown, that phosphomimicking mutant S58E cannot be considered a sufficient replacement for phosphorylated 14-3-3ζ at S58. Not only does their stability differ in various conditions, with overall better stability of S58E, but their intrinsic fluorescence behaves differently as well.
ER  -

NÁPLAVOVÁ, Alexandra, Aneta KOZELEKOVÁ a Jozef HRITZ. Phosphomimicking mutants: why to be careful. In \textit{XX. Workshop of Biophysical Chemists and Electrochemists}. 2020. ISBN~978-80-210-9655-4.

Podrobný výpis o publikaci