Expression of N-formylated proteins in Escherichia coli |
| |
Authors: | Spector Shari Flynn Julia M Tidor Bruce Baker Tania A Sauer Robert T |
| |
Institution: | Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. |
| |
Abstract: | In bacteria, protein expression initiates with a formyl-methionine group. Addition of the antibiotic actinonin, a known peptide deformylase inhibitor, at the time of induction of protein expression results in the retention of the formyl group by the overexpressed protein. In addition, because deformylation is a prerequisite for removal of the initiating methionine, this post-translational processing step is also prevented by actinonin, and the N-formyl methionine residue is retained by proteins from which it is normally removed. We have demonstrated the applicability of this system for obtaining N-modified forms of several different proteins and use one of these modified molecules to show that the N-terminal amino group is not required for ClpXP degradation of proteins bearing an N-terminal recognition signal. |
| |
Keywords: | Protein modification α -Amino group |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|