Truncation of recombinant vimentin by ompT Identification of a short motif in the head domain necessary for assembly of type III intermediate filament proteins

FEBS Letters

Hatzfeld, Mechthild¹  Weber, Klaus¹  Dodemont, Huub¹  Plessmann, Uwe¹ 

[1] Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, D-3400 Goettingen, Germany

关键词: Intermediate filament;    ompT;    Protease;    Sequence motif;    Vimentin;   

DOI  :  10.1016/0014-5793(92)80450-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recombinant vimentin expressed in E. coli JM 101 cells is cleaved after cell lysis between arginines 11 and 12. The truncated vimentin is assembly incompetent. Expression of the same cDNA construct in BL21 cells, which lack the protease ompT, provides intact and polymerization-competent vimentin. The ompT cleavage site is contained in a short sequence motif (YRRMF) shared by the head domains of type III and IV intermediate filament (IF) proteins. We propose that a related motif present in the N-terminal 32 residues of λCII acounts for the known IF formation of a fusion protein formed with a truncated GFAP.

【 授权许可】

Unknown