Fructose-1,6-bisphosphate aldolase preferentially associates to glyceraldehyde-3-phosphate dehydrogenase in a mixture of cytosolic proteins as revealed by fluorescence energy transfer measurements.

TitleFructose-1,6-bisphosphate aldolase preferentially associates to glyceraldehyde-3-phosphate dehydrogenase in a mixture of cytosolic proteins as revealed by fluorescence energy transfer measurements.
Publication TypeJournal Article
Year of Publication1990
AuthorsTompa, P., and J. Batke
JournalBiochem Int
Volume20
Issue3
Pagination487-94
Date Published1990
ISSN0158-5231
KeywordsAnimals, Bicyclo Compounds, Cytosol, Energy Transfer, Fluorescein-5-isothiocyanate, Fluoresceins, Fluorescent Dyes, Fructose-Bisphosphate Aldolase, Glyceraldehyde-3-Phosphate Dehydrogenases, Protein Binding, Proteins, Rabbits, Spectrometry, Fluorescence, Thiocyanates
Abstract

Fluorescence energy transfer measurements were implemented for demonstrating the specific character of the interaction between aldolase and glyceraldehyde-3-phosphate dehydrogenase. The enzymes, labeled with monobromobimane (donor) and fluorescein isothiocyanate (acceptor), respectively, were mixed into a cytosol preparation and energy transfer between the two fluorophores was observed to develop. This observation reflecting a contact between the two enzymes, suggests that despite the presence of a multitude of potential macromolecular partners glyceraldehyde-3-phosphate dehydrogenase and aldolase are capable of recognizing each other in the cytoplasm. The idea that in vivo associations of metabolically sequential enzymes may be of physiological benefits is consistent with this result.

Alternate JournalBiochem. Int.
PubMed ID2111996