Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  The ATP-ase cycle of the endoplasmic chaperone GRP94

Frey, S., Leskovar, A., Reinstein, J., & Buchner, J. (2007). The ATP-ase cycle of the endoplasmic chaperone GRP94. The Journal of Biological Chemistry, 282(49), 35612-35620. doi:10.1074/jbc.M704647200.

Item is

Basisdaten

einblenden: ausblenden:
Genre: Zeitschriftenartikel
Alternativer Titel : The ATP-ase cycle of the endoplasmic chaperone GRP94

Dateien

einblenden: Dateien
ausblenden: Dateien
:
JBiolChem_282_2007_35612.pdf (beliebiger Volltext), 309KB
 
Datei-Permalink:
-
Name:
JBiolChem_282_2007_35612.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Eingeschränkt (Max Planck Institute for Medical Research, MHMF; )
MIME-Typ / Prüfsumme:
application/pdf
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-

Externe Referenzen

einblenden:
ausblenden:
externe Referenz:
http://www.jbc.org/content/282/49/35612.full.pdf (beliebiger Volltext)
Beschreibung:
-
OA-Status:
externe Referenz:
https://dx.doi.org/10.1074/jbc.M704647200 (beliebiger Volltext)
Beschreibung:
-
OA-Status:

Urheber

einblenden:
ausblenden:
 Urheber:
Frey, Stephan, Autor
Leskovar, Adriane1, Autor           
Reinstein, Jochen1, Autor           
Buchner, Johannes, Autor
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Inhalt

einblenden:
ausblenden:
Schlagwörter: -
 Zusammenfassung: Grp94, the Hsp90 paralog of the endoplasmic reticulum, plays a crucial role in protein secretion. Like cytoplasmic Hsp90, Grp94 is regulated by nucleotide binding to its N-terminal domain. However, the question of whether Grp94 hydrolyzes ATP was controversial. This sets Grp94 apart from other members of the Hsp90 family where a slow but specific turnover of ATP has been unambiguously established. In this study we aimed at analyzing the nucleotide binding properties and the potential ATPase activity of Grp94. We show here that Grp94 has an ATPase activity comparable with that of yeast Hsp90 with a k(cat) of 0.36 min(-1) at 25 degrees C. Kinetic and equilibrium constants of the partial reactions of the ATPase cycle were determined using transient kinetic methods. Nucleotide binding appears to be tighter compared with other Hsp90s investigated, with dissociation constants (K(D)) of approximately 4 microm for ADP, ATP, and AMP-PCP. Interestingly, all nucleotides and inhibitors (radicicol, 5'-N-ethylcarboxamidoadenosine) studied here bind with similar rate constants for association (0.2-0.3 x 10(6) M(-1) s(-1)). Furthermore, there is a marked difference from cytosolic Hsp90s in that after binding, the ATP molecule does not seem to become trapped by conformational changes in Grp94. Grp94 stays predominantly in the open state concerning the nucleotide-binding pocket as evidenced by kinetic analyses. Thus, Grp94 shows mechanistically important differences in the interaction with adenosine nucleotides, but the basic hydrolysis reaction seems to be conserved between cytosolic and endoplasmic members of the Hsp90 family.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2007-09-142007-06-062007-10-092007-10-092007-12-07
 Publikationsstatus: Erschienen
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 665076
DOI: 10.1074/jbc.M704647200
URI: http://www.ncbi.nlm.nih.gov/pubmed/17925398?dopt%3DAbstract
Anderer: 7025
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: The Journal of Biological Chemistry
  Andere : JBC
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Seiten: - Band / Heft: 282 (49) Artikelnummer: - Start- / Endseite: 35612 - 35620 Identifikator: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1