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GroE facilitates refolding of citrate synthase by suppressing aggregation

Title data

Buchner, Johannes ; Schmidt, Marion ; Fuchs, Miriam ; Jaenicke, Rainer ; Rudolph, Rainer ; Schmid, Franz X. ; Kiefhaber, Thomas:
GroE facilitates refolding of citrate synthase by suppressing aggregation.
In: Biochemistry. Vol. 30 (12 February 1991) Issue 6 . - pp. 1586-1591.
ISSN 0006-2960
DOI: https://doi.org/10.1021/bi00220a020

Abstract in another language

The molecular chaperone GroE facilitates correct protein folding in vivo and in vitro. The mode of action of GroE was investigated by using refolding of citrate synthase as a model system. In vitro denaturation of this dimeric protein is almost irreversible, since the refolding polypeptide chains aggregate rapidly, as shown directly by a strong, concentration-dependent increase in light scattering. The yields of reactivated citrate synthase were strongly increased upon addition of GroE and MgATP. GroE inhibits aggregation reactions that compete with correct protein folding, as indicated by specific suppression of light scattering. GroEL rapidly forms a complex with unfolded or partially folded citrate synthase molecules. In this complex the refolding protein is protected from aggregation. Addition of GroES and ATP hydrolysis is required to release the polypeptide chain bound to GroEL and to allow further folding to its final, active state.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 1671555
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 13 May 2015 06:19
Last Modified: 13 May 2015 06:19
URI: https://eref.uni-bayreuth.de/id/eprint/13438