Replacement of ATP with ADP affects the dynamic and conformational properties of actin monomer

Balázs Gaszner, M. Nyitrai, Nóra Hartvig, T. Kőszegi, B. Somogyi, J. Belágyi

Research output: Article

14 Citations (Scopus)

Abstract

The effect of the replacement of ATP with ADP on the conformational and dynamic properties of the actin monomer was investigated, by means of electron paramagnetic resonance (EPR) and fluorescence spectroscopic methods. The measurement of the ATP concentration during these experiments provided the opportunity to estimate the time dependence of ADP-Mg-G-actin concentration in the samples. According to the results of the fluorescence resonance energy transfer experiments, the Gln-41 and Cys-374 residues are closer to each other in the ADP-Mg-G- actin than in the ATP-Mg-G-actin. The fluorescence resonance energy transfer efficiency increased simultaneously with the ADP- G-actin concentration and reached its maximum value within 30 min at 20 °C. The EPR data indicate the presence of an ADPMg-G-actin population that can be characterized by an increased rotational correlation time, which is similar to the one observed in actin filaments, and exists only transiently. We suggest that the conformational transitions, which were reflected by our EPR data, were coupled with the transient appearance of short actin oligomers during the nucleotide exchange. Besides these relatively fast conformational changes, there is a slower conformational transition that could be detected several hours after the initiation of the nucleotide exchange.

Original languageEnglish
Pages (from-to)12885-12892
Number of pages8
JournalBiochemistry
Volume38
Issue number39
DOIs
Publication statusPublished - szept. 28 1999

Fingerprint

Electron Spin Resonance Spectroscopy
Adenosine Diphosphate
Actins
Fluorescence Resonance Energy Transfer
Adenosine Triphosphate
Monomers
Nucleotides
Paramagnetic resonance
Actin Cytoskeleton
Fluorescence
Population
ADP-G-actin
Oligomers
Experiments

ASJC Scopus subject areas

  • Biochemistry

Cite this

Replacement of ATP with ADP affects the dynamic and conformational properties of actin monomer. / Gaszner, Balázs; Nyitrai, M.; Hartvig, Nóra; Kőszegi, T.; Somogyi, B.; Belágyi, J.

In: Biochemistry, Vol. 38, No. 39, 28.09.1999, p. 12885-12892.

Research output: Article

@article{dfc20c93254a4683a5c61d8368539e14,
title = "Replacement of ATP with ADP affects the dynamic and conformational properties of actin monomer",
abstract = "The effect of the replacement of ATP with ADP on the conformational and dynamic properties of the actin monomer was investigated, by means of electron paramagnetic resonance (EPR) and fluorescence spectroscopic methods. The measurement of the ATP concentration during these experiments provided the opportunity to estimate the time dependence of ADP-Mg-G-actin concentration in the samples. According to the results of the fluorescence resonance energy transfer experiments, the Gln-41 and Cys-374 residues are closer to each other in the ADP-Mg-G- actin than in the ATP-Mg-G-actin. The fluorescence resonance energy transfer efficiency increased simultaneously with the ADP- G-actin concentration and reached its maximum value within 30 min at 20 °C. The EPR data indicate the presence of an ADPMg-G-actin population that can be characterized by an increased rotational correlation time, which is similar to the one observed in actin filaments, and exists only transiently. We suggest that the conformational transitions, which were reflected by our EPR data, were coupled with the transient appearance of short actin oligomers during the nucleotide exchange. Besides these relatively fast conformational changes, there is a slower conformational transition that could be detected several hours after the initiation of the nucleotide exchange.",
author = "Bal{\'a}zs Gaszner and M. Nyitrai and N{\'o}ra Hartvig and T. Kőszegi and B. Somogyi and J. Bel{\'a}gyi",
year = "1999",
month = "9",
day = "28",
doi = "10.1021/bi990748y",
language = "English",
volume = "38",
pages = "12885--12892",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "39",

}

TY - JOUR

T1 - Replacement of ATP with ADP affects the dynamic and conformational properties of actin monomer

AU - Gaszner, Balázs

AU - Nyitrai, M.

AU - Hartvig, Nóra

AU - Kőszegi, T.

AU - Somogyi, B.

AU - Belágyi, J.

PY - 1999/9/28

Y1 - 1999/9/28

N2 - The effect of the replacement of ATP with ADP on the conformational and dynamic properties of the actin monomer was investigated, by means of electron paramagnetic resonance (EPR) and fluorescence spectroscopic methods. The measurement of the ATP concentration during these experiments provided the opportunity to estimate the time dependence of ADP-Mg-G-actin concentration in the samples. According to the results of the fluorescence resonance energy transfer experiments, the Gln-41 and Cys-374 residues are closer to each other in the ADP-Mg-G- actin than in the ATP-Mg-G-actin. The fluorescence resonance energy transfer efficiency increased simultaneously with the ADP- G-actin concentration and reached its maximum value within 30 min at 20 °C. The EPR data indicate the presence of an ADPMg-G-actin population that can be characterized by an increased rotational correlation time, which is similar to the one observed in actin filaments, and exists only transiently. We suggest that the conformational transitions, which were reflected by our EPR data, were coupled with the transient appearance of short actin oligomers during the nucleotide exchange. Besides these relatively fast conformational changes, there is a slower conformational transition that could be detected several hours after the initiation of the nucleotide exchange.

AB - The effect of the replacement of ATP with ADP on the conformational and dynamic properties of the actin monomer was investigated, by means of electron paramagnetic resonance (EPR) and fluorescence spectroscopic methods. The measurement of the ATP concentration during these experiments provided the opportunity to estimate the time dependence of ADP-Mg-G-actin concentration in the samples. According to the results of the fluorescence resonance energy transfer experiments, the Gln-41 and Cys-374 residues are closer to each other in the ADP-Mg-G- actin than in the ATP-Mg-G-actin. The fluorescence resonance energy transfer efficiency increased simultaneously with the ADP- G-actin concentration and reached its maximum value within 30 min at 20 °C. The EPR data indicate the presence of an ADPMg-G-actin population that can be characterized by an increased rotational correlation time, which is similar to the one observed in actin filaments, and exists only transiently. We suggest that the conformational transitions, which were reflected by our EPR data, were coupled with the transient appearance of short actin oligomers during the nucleotide exchange. Besides these relatively fast conformational changes, there is a slower conformational transition that could be detected several hours after the initiation of the nucleotide exchange.

UR - http://www.scopus.com/inward/record.url?scp=0033613174&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033613174&partnerID=8YFLogxK

U2 - 10.1021/bi990748y

DO - 10.1021/bi990748y

M3 - Article

C2 - 10504259

AN - SCOPUS:0033613174

VL - 38

SP - 12885

EP - 12892

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 39

ER -