The Folding and Assembly Pathway of Tumour Necrosis Factor TNFalpha, a Globular Trimeric Protein
- 1 July 1995
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 231 (2) , 381-387
- https://doi.org/10.1111/j.1432-1033.1995.tb20710.x
Abstract
The mechanisms of folding and assembly of the globular, trimeric protein tumour necrosis factor-alpha (TNF) were studied by chemical cross-linking. This revealed the rapid accumulation of a dimeric intermediate. Under the conditions of renaturation used, formation of the trimer is complete within six minutes. The kinetics of change of intrinsic and 8-anilino-1-naphthalene sulfonic acid fluorescence are first order and, combined with the kinetics of association, reveal the presence of folding steps both before and subsequent to formation of the trimer. Results from gel exclusion chromatography and kinetics, together with the existence of an acid-induced molten globule, support the conclusion that TNF folds and assembles through a trimeric molten globule.Keywords
This publication has 32 references indexed in Scilit:
- Tumour necrosis factor is in equilibrium with a trimeric molten globule at low pHFEBS Letters, 1994
- Prolyl Isomerase: Enzymatic Catalysis of Slow Protein-Folding ReactionsAnnual Review of Biophysics, 1993
- In vitro folding pathway of phage P22 tailspike proteinBiochemistry, 1991
- Evidence for a molten globule state as a general intermediate in protein foldingFEBS Letters, 1990
- Self-assembly of apoferritin from horse spleen after reversible chemical modification with 2,3-dimethylmaleic anhydrideBiochemistry, 1988
- Tumour necrosis factor is a compact trimerFEBS Letters, 1987
- Dissociation and in vitro reconstitution of bovine liver uridine diphosphoglucose dehydrogenase. The paired subunit nature of the enzymeBiochemistry, 1986
- Reassociation of dimeric cytoplasmic malate dehydrogenase is determined by slow and very slow folding reactionsBiochemistry, 1986
- Mechanism and Specificity of Reconstitution of Dimeric Lactate Dehydrogenase fromLimulus polyphemusBiological Chemistry Hoppe-Seyler, 1985
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970