Journal
FEBS JOURNAL
Volume 272, Issue 11, Pages 2892-2900Publisher
WILEY
DOI: 10.1111/j.1742-4658.2005.04710.x
Keywords
chemical assisted fragmentation (CAF); mass spectrometry; protein modification; signal peptidase
Categories
Ask authors/readers for more resources
Although the annotation of the complete genome sequence of Mycoplasma pneumoniae did not reveal a bacterial type I signal peptidase (SPase I) we showed experimentally that such an activity must exist in this bacterium, by determining the N-terminus of the N-terminal gene product P40 of MPN142, formerly called ORF6 gene. Combining mass spectrometry with a method for sulfonating specifically the free amino terminal group of proteins, the cleavage site for a typical signal peptide was located between amino acids 25 and 26 of the P40 precursor protein. The experimental results were in agreement with the cleavage site predicted by computational methods providing experimental confirmation for these theoretical analyses.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available