Phosphate-buffered native gel electrophoresis of E-Coli H-NS

Abstract

Histone-like nucleoid structuring protein (H-NS) is a global regulator in enteric bacteria and other bacteria. It has been reported that H-NS has no modifications for its activity. Even though H-NS is called histone-like protein, it is acidic, contrary to the basic eukaryotic histones. Here, we report that there were mobility differences for various sources of H-NS seen in sodium phosphate-buffered native gel electrophoresis. We examined various native gel electrophoresis conditions using the wild-type E. coli (MG1655), three H-NS mutants (two were H-NS knockout mutants), and the E. coli BL21 overexpressing H-NS (BL21 (DE3)/pPD3).