Overexpression of an archaeal geranylgeranyl diphosphate synthase in Escherichia coli cells

Biosci Biotechnol Biochem. 1998 Jun;62(6):1243-6. doi: 10.1271/bbb.62.1243.


An archaeal geranylgeranyl diphosphate synthase was overexpressed in Escherichia coli cells as fusion proteins. These fusion proteins retained their thermostability and had higher specific activity than did a partially purified native enzyme Previously reported. We purified 24.3 mg of MBP (maltose-binding protein)-fusion protein and 5.4 mg of GST (glutathione S-transferase)-fusion protein from a one-liter culture of E. coli. The MBP-fusion proteins existed in dimer, tetramer, octamer, or dodecamer form, and their product specificities were altered according to the oligomerization. The MBP-fusion protein has protease-sensitive sites in the portion corresponding to geranylgeranyl diphosphate synthase.

MeSH terms

  • ATP-Binding Cassette Transporters*
  • Alkyl and Aryl Transferases / biosynthesis
  • Alkyl and Aryl Transferases / genetics*
  • Bacterial Proteins / isolation & purification
  • Carrier Proteins / isolation & purification
  • Chemical Fractionation
  • Escherichia coli
  • Escherichia coli Proteins*
  • Farnesyltranstransferase
  • Gene Expression
  • Maltose-Binding Proteins
  • Monosaccharide Transport Proteins*
  • Recombinant Fusion Proteins / biosynthesis
  • Sulfolobus acidocaldarius


  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Carrier Proteins
  • Escherichia coli Proteins
  • Maltose-Binding Proteins
  • Monosaccharide Transport Proteins
  • Recombinant Fusion Proteins
  • maltose transport system, E coli
  • Alkyl and Aryl Transferases
  • Farnesyltranstransferase

Associated data

  • GENBANK/D28748