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Lysine acetylation regulates DNA‐binding by Mycobacterium tuberculosis HU (MtHU). Atomic force microscopy reveals that MtHU binds to relaxed plasmid DNA to form condensed structures (top, middle). Acetylation of MtHU, on long carboxyl terminal extension similar to eukaryotic histones, leads to formation of MtHU‐DNA fi laments (top right, and bottom panel). For details, see the article by Ghosh et al. on pp. 577–588 of this issue.
Publication year - 2016
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13184
Subject(s) - acetylation , dna , histone , lysine , biology , plasmid , mycobacterium tuberculosis , atomic force microscopy , microbiology and biotechnology , genetics , nanotechnology , tuberculosis , gene , materials science , amino acid , medicine , pathology