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GroEL-assisted dehydrogenase folding mediated by coenzyme is ATP-independent.
Biochem Biophys Res Commun. 2001 Jul 13; 285(2):277-82.BB

Abstract

It has been commonly accepted that GroEL functions as a chaperone by modulation of its affinity for folding intermediates through binding and hydrolysis of ATP. However, we have found that NAD, as a coenzyme of d-glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also stimulates the discharge of GAPDH folding intermediate from its stable complex with GroEL formed in the absence of ATP and assists refolding with the same yield as ATP/Mg(2+) does. The reactivation further increases when ATP is also present, but addition of Mg(2+) has no more effect. NADP, a coenzyme of glucose-6-phosphate dehydrogenase, also releases its folding intermediates from GroEL and increases reactivation. Different from ATP, NAD triggers the release of GAPDH intermediates bound by GroEL via binding with GAPDH itself but not with GroEL, and the released intermediates all folded to native molecules without the formation of aggregation. The collaborative effects of coenzyme and GroEL mediate GroEL-assisted dehydrogenase folding in an ATP-independent way.

Authors+Show Affiliations

National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing 100101, China.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11444838

Citation

Zhang, S, et al. "GroEL-assisted Dehydrogenase Folding Mediated By Coenzyme Is ATP-independent." Biochemical and Biophysical Research Communications, vol. 285, no. 2, 2001, pp. 277-82.
Zhang S, Li J, Wang CC. GroEL-assisted dehydrogenase folding mediated by coenzyme is ATP-independent. Biochem Biophys Res Commun. 2001;285(2):277-82.
Zhang, S., Li, J., & Wang, C. C. (2001). GroEL-assisted dehydrogenase folding mediated by coenzyme is ATP-independent. Biochemical and Biophysical Research Communications, 285(2), 277-82.
Zhang S, Li J, Wang CC. GroEL-assisted Dehydrogenase Folding Mediated By Coenzyme Is ATP-independent. Biochem Biophys Res Commun. 2001 Jul 13;285(2):277-82. PubMed PMID: 11444838.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - GroEL-assisted dehydrogenase folding mediated by coenzyme is ATP-independent. AU - Zhang,S, AU - Li,J, AU - Wang,C C, PY - 2001/7/11/pubmed PY - 2001/8/17/medline PY - 2001/7/11/entrez SP - 277 EP - 82 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 285 IS - 2 N2 - It has been commonly accepted that GroEL functions as a chaperone by modulation of its affinity for folding intermediates through binding and hydrolysis of ATP. However, we have found that NAD, as a coenzyme of d-glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also stimulates the discharge of GAPDH folding intermediate from its stable complex with GroEL formed in the absence of ATP and assists refolding with the same yield as ATP/Mg(2+) does. The reactivation further increases when ATP is also present, but addition of Mg(2+) has no more effect. NADP, a coenzyme of glucose-6-phosphate dehydrogenase, also releases its folding intermediates from GroEL and increases reactivation. Different from ATP, NAD triggers the release of GAPDH intermediates bound by GroEL via binding with GAPDH itself but not with GroEL, and the released intermediates all folded to native molecules without the formation of aggregation. The collaborative effects of coenzyme and GroEL mediate GroEL-assisted dehydrogenase folding in an ATP-independent way. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/11444838/GroEL_assisted_dehydrogenase_folding_mediated_by_coenzyme_is_ATP_independent_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(01)95182-4 DB - PRIME DP - Unbound Medicine ER -