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In vivo suppression of phytochrome aggregation by the GroE chaperonins in Escherichia coli (1993)

Edgerton, Michael D. ; Santos, Michael O. ; Jones, Alan M.

Springer

Plant molecular biology 21 (1993), S. 1191-1194

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ISSN: 1573-5028

Keywords: phytochrome ; chaperonins ; protein expression

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00023616

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