Formation and quantification of protein complexes between peroxisomal alcohol oxidase and GroEL Journal Article


Authors: Evers, M. E.; Langer, T.; Harder, W.; Hartl, F. U.; Veenhuis, M.
Article Title: Formation and quantification of protein complexes between peroxisomal alcohol oxidase and GroEL
Abstract: We have studied the use of yeast peroxisomal alcohol oxidase (AO) as a model protein for in vitro binding by GroEL. Dilution of denatured AO in neutral buffer leads to aggregation of the protein, which is prevented by the addition of GroEL. Formation of complexes between GroEL and denatured AO was demonstrated by a gel-shift assay using non-denaturing polyacrylamide gel electrophoresis, and quantified by laser-densitometry of the gels. In the presence of MgAMP-PNP or MgADP the affinity of GroEL for AO was enhanced. Under these conditions up to 70% of the purified GroEL formed a complex with this protein. Release was stimulated at room temperature by MgATP, and was further enhanced by addition of GroES.
Keywords: saccharomyces-cerevisiae; alcohol oxidase; atp; groel; hsp; hansenula-polymorpha; ribulosebisphosphate-carboxylase; nondenaturing gel electrophoresis; peroxisomal matrix protein; protein complex formation
Journal Title: FEBS Letters
Volume: 305
Issue: 1
ISSN: 0014-5793
Publisher: Wiley Blackwell  
Date Published: 1992-06-22
Start Page: 51
End Page: 54
Language: English
ACCESSION: WOS:A1992JB92300012
DOI: 10.1016/0014-5793(92)80653-x
PROVIDER: wos
PUBMED: 1353025
Notes: Source: Wos
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  1. F. Ulrich Hartl
    75 Hartl