In vivo suppression of phytochrome aggregation by the GroE chaperonins in Escherichia coli.
When expressed in Escherichia coli, a truncated form of phytochrome (oat PHYA AP3 residues 464-1129) self associates to form a series of products ranging in size from monomers to aggregates of greater than 20 subunits. When these same phytochrome sequences are coexpressed with the chaperonins GroEL and GroES, the truncated phytochrome migrates as a native-like dimer in size exclusion chromatography and no higher-order aggregates were detected. GroEL and GroES inhibition of phytochrome aggregation in E. coli presumably occurs via the suppression of folding pathways leading to incorrectly folded phytochrome.
Edgerton
M D
MD
Department of Biology, University of North Carolina, Chapel Hill 27599-3280.
Santos
M O
MO
Jones
A M
AM
D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D018833:Chaperonins; D003001:Cloning, Molecular; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins / Q000235:genetics* / Q000378:metabolism; D015151:Immunoblotting; D010834:Phytochrome / Q000235:genetics* / Q000378:metabolism; D017510:Protein Folding
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C028715:GroE protein, E coli; D006360:Heat-Shock Proteins; D010834:Phytochrome; D018833:Chaperonins