期刊
FEBS JOURNAL
卷 272, 期 11, 页码 2892-2900出版社
WILEY
DOI: 10.1111/j.1742-4658.2005.04710.x
关键词
chemical assisted fragmentation (CAF); mass spectrometry; protein modification; signal peptidase
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.
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