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Titolo:
Oxidative modification of nucleoside diphosphate kinase and its identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
Autore:
Song, EJ; Kim, YS; Chung, JY; Kim, E; Chae, SK; Lee, KJ;
Indirizzi:
Ewha Womans Univ, Ctr Cell Signaling Res, Div Mol Life Sci, Seoul 120750, South Korea Ewha Womans Univ Seoul South Korea 120750 Sci, Seoul 120750, South Korea Ewha Womans Univ, Coll Pharm, Seoul 120750, South Korea Ewha Womans Univ Seoul South Korea 120750 arm, Seoul 120750, South Korea Paichai Univ, Res Ctr Biomed Resources, Taejon 302735, South Korea PaichaiUniv Taejon South Korea 302735 urces, Taejon 302735, South Korea Paichai Univ, Div Life Sci, Taejon 302735, South Korea Paichai Univ Taejon South Korea 302735 e Sci, Taejon 302735, South Korea
Titolo Testata:
BIOCHEMISTRY
fascicolo: 33, volume: 39, anno: 2000,
pagine: 10090 - 10097
SICI:
0006-2960(20000822)39:33<10090:OMONDK>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST SACCHAROMYCES-CEREVISIAE; TRANSCRIPTION FACTOR; TUMOR-METASTASIS; PROTEIN OXIDATION; LEUKEMIA-CELLS; NM23; GENE; STRESS; DIFFERENTIATION; PROTEOLYSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Lee, KJ Ewha Womans Univ, Ctr Cell Signaling Res, Div Mol Life Sci, Seoul 120750, South Korea Ewha Womans Univ Seoul South Korea 120750 ul 120750, South Korea
Citazione:
E.J. Song et al., "Oxidative modification of nucleoside diphosphate kinase and its identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry", BIOCHEM, 39(33), 2000, pp. 10090-10097

Abstract

Nucleoside diphosphate kinase (NDPK, Nm23) has been implicated as a multifunctional protein. However, the regulatory mechanism of NDPK is poorly understood. We have examined the modification of NDPK in oxidative stresses. Wefound that oxidative stresses including diamide and H2O2 treatment cause disulfide cross-linking of NDPK inside cells. This cross-linking was reversible in response to mild oxidative stress, and irreversible to strong stress. This suggests that disulfide cross-linked NDPK may be a possible mechanism in the modification of cellular regulation. To confirm this idea, oxidative modification of NDPK has been performed in vitro using purified human NDPK H2O2 inactivated the nucleoside diphosphate (NDP) kinase activity of NDPK by producing intermolecular disulfide bonds. Disulfide cross-linking of NDPK also dissociated the native hexameric structure into a dimeric form. The oxidation sites were identified by the analysis of tryptic peptides of oxidized NDPK, using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Intermolecular cross-linking between Cys109-Cys109, which is highly possible based on the X-ray crystal structureof NDPK-A, and oxidations of four methionine residues were identified in H2O2-treated NDPK. This cross-linkng was confirmed using mutant C109A (NDPK-A(C109A)) which had similar enzymatic activity as a wild NDPK-A. Mutant NDPK-A(C109A) was not cross-linked and was not easily denatured by the oxidant. Therefore, enzymatic activity and the quaternary structure of NDPK appearto be regulated by cross-linking with oxidant. These findings suggest one of the regulatory mechanisms of NDPK in various cellular processes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 04:00:24