The exbB locus of Escherichia coli is involved in the uptake of certain iron(III) siderophore compounds, of vitamin B12 and of certain colicins. Outer membrane receptor proteins are essential constituents of the corresponding uptake systems. The DNA carrying the exbB locus was cloned into pACYC184 a
Cloning and expression in Escherichia coli K-12 of the biosynthetic dehydroquinase function of the arom cluster gene from the eucaryote, Aspergillus nidulans
โ Scribed by Kinghorn, James R. ;Hawkins, Alastair R.
- Publisher
- Springer
- Year
- 1982
- Tongue
- English
- Weight
- 817 KB
- Volume
- 186
- Category
- Article
- ISSN
- 0026-8925
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โฆ Synopsis
A 1.35 Md DNA HindIII fragment containing part of the arom gene cluster or cluster gene of Aspergillus nidulans encoding biosynthetic dehydroquinase (5-dehydroquinate hydrolyase) has been cloned in plasmid pBR322 on the basis of functional expression in Escherichia coli. The fungal fragment on pBR322, designated pHK29, complements a corresponding E. coli dehydroquinase structural gene (aroD) mutation. pHK29 contains one BamHI, HpaII, PstI, SmaI, XhoI and surprisingly, one HindIII site since pHK29 hybrid Aspergillus DNA is a HindIII fragment itself. The biosynthetic dehydroquinase activity extracted from E. coli strains, containing pHK29, had properties similar to those of the enzyme activity from Aspergillus. The protein specified by pHK29 appears to be 80 kd. No increase of dehydroquinase activity was found in polynucleotide phosphorylase deficient strains (pnp) of E. coli.
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