HupA (red) expressing E. coli with DIC (green) overlaid in confocal microscopy
The heat-stable protein HU was isolated first by Josette Rouviere-Yaniv and Gros in 1975 in a study where they systematically screened using an DNA-binding affinity-purification method for heat-stable proteins from E. coli cell extracts (1). This protein has been implicated in DNA replication initiation and cell cycle control (2,3). More recently the nucleoid binding HU protein from Mycobacterium tuberculosis
has been crystallized and the structure used to develop a small molecule which binds to HU and inhibits Mtb growth (4). This would appear to suggest surprisingly large number of physiologically critical bacterial proteins are still to be characterized that could help in the newly coined “post antibiotic era”.
REFERENCES
- J Rouvière-Yaniv and F Gros (1975) Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli. Proc Natl Acad Sci U S A. 1975 Sep; 72(9): 3428–3432.
- Jaffe A, Vinella D, D’Ari R. (1997) The Escherichia coli histone-like protein HU affects DNA initiation, chromosome partitioning via MukB, and cell division via MinCDE. J Bacteriol. 179(11):3494-9.
- Jason Kahn’s Lab (U. Maryland, USA) on Prokaryotic DNA Replication
- Bhowmick,T., Ghosh, S., Ramagopal,U.A.,Dey, D. Ramakumar,S. and Nagaraja,V. (2014) Targeting Mycobacterium tuberculosis nucleoid associated protein HU by structure based inhibitors. Nature Communications. 5:4124