Co-expression of gene 31 and 23 products of bacteriophage T4.
Folding of the major capsid protein of bacteriophage T4 encoded by gene 23 is aided by Escherichia coli GroEL chaperonin and phage co-chaperonin gp31. In the absence of gene product (gp) 31, aggregates of recombinant gp23 accumulate in the cell similar to inclusion bodies. These aggregates can be solubilized with 6 M urea. However, the protein cannot form regular structures in solution. A system of co-expression of gp31 and gp23 under the control of phage T7 promoter in E. coli cells has been constructed. Folding of entire-length gp23 (534 amino acid residues) in this system results in the correctly folded recombinant gp23, which forms long regular structures (polyheads) in the cell.
Kurochkina
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LP
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117871, Russia. vvm@ibch.siobc.ras.ru.
Mesyanzhinov
V V
VV
D017123:Bacteriophage T7 / Q000235:genetics; D001483:Base Sequence; D002213:Capsid / Q000235:genetics* / Q000378:metabolism; D036022:Capsid Proteins; D003001:Cloning, Molecular; D017931:DNA Primers; D008854:Microscopy, Electron; D011401:Promoter Regions, Genetic; D017510:Protein Folding; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics*
D036022:Capsid Proteins; D017931:DNA Primers; D011994:Recombinant Proteins; D014764:Viral Proteins; C063473:gene 31 protein, Enterobacteria phage T4; C064517:gp23 protein, Bacteriophage T4