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Several other nucleoside-binding proteins bind to their substrates by sandwiching the nucleobase between aromatic residues (Suzuki et al., 2004; Monecke et al., 2014).
However, it has to be noted that many hydrolases actively bind to their substrates via carbohydrate-binding modules and therefore can only be partially detected in culture supernatants.
Ca2+-induced rigidity of tandem Ig-like repeats in large adhesins might be a general mechanism used by bacteria to bind to their substrates and help colonize specific niches.
Previous work from our group on the individual LysMAcmA (p I 10.0) and PMBMTH719 (p I 10.6) domains has shown that both bind to their substrates at a pH close to their respective p I values (Buist et al. 1995; Steen et al. 2003, 2005; Visweswaran et al. 2011a).
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Making use of short-distance energy-transfer mechanisms, only the fluorescence from those proteins that bind to their substrate is activated.
On the other hand, ubiquitin-like molecules (Ubls), such as SUMO, are also covalently bound to their substrates, and thus are conjugated, deconjugated and recognized by specific enzymes and their targets [8], [9].
These transporters bind to their respective substrates and catalyze their efflux from cancer cells, thereby lowering the intracellular concentrations of the substrates and thus attenuating or even abolishing their efficacy.
Despite sharing a conserved domain architecture, chromatin remodelers differ significantly in how they bind to their nucleosomal substrates.
Previous studies suggested that IKKε and TBK1 bind to their respective substrates through a sequence that includes a ubiquitin-like domain (ULD) proximal to their kinase domain.
Scaffold proteins are biologically inert but bind to their respective substrates through the action of auxiliary phosphatases and protein kinases, thus exerting inflammatory response effects.
We suggest the Ca2+-induced rigidity in the large repetitive extender domains of RTX adhesins is a general mechanism used by Gram-negative bacteria, including pathogens, to bind to their specific substrates.
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