MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint sharadamma-2011-1 Synergy between the N-terminal and C-terminal domains of Mycobacterium tuberculosis HupB is essential for high-affinity binding, DNA supercoiling and inhibition of RecA-promoted strand exchange. in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Sharadamma N., Khan K., Kumar S., Patil KN., Hasnain SE., Muniyappa K. FEBS J. (1742-464X) 2011 Only protein-protein interactions imex curation dbh_myctu DNA-binding protein HU homolog hup hlp hupB lbp21 21 kDa laminin-2-binding protein 28 kDa iron-regulated protein Histone-like protein MTCY349.01 Rv2986c protein protein myctu Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVSGAQRLPAEGPAVKRGVGASAAKKVAKKAPAKKATKAAKKAATKAPARKAATKAPAKKAATKAPAKKAVKATKSPAKKVTKAVKKTAVKASVRKAATKAPAKKAAAKRPATKAPAKKATARRGRK mint hup-1 1167511 dbh_myctu hupB 1167512 weight silver stain molecular weight estimation by silver staining weight silver stain unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false F2 mint The oligomerization state of HupB and HupBMtbN was examined by chemical cross-linking, we observed a slower migrating band corresponding to a dimer of HupB or HupBMtbN (Fig. 2, lanes 3 6, left and right panels respectively) whose intensity increased with increasing concentrations of glutaraldehyde. Taken together, these results suggest that both HupB and HupBMtbN occur as dimers, and exclude the possible existence of protein aggregates in solution