IMPLICATION OF RbsD OF THE D-RIBOSE HIGH-AFFINITY TRANSPORT SYSTEM OF ESCHERICHIA COLI AS A REGULATOR OF RIBOKINASE ACTIVITY

The D-ribose high-affinity transport operon (RbsDACBKR) of Escherichia coli encodes the proteins necessary for high-affinity transport and utilization of D-ribose. rbsD encodes a 15 kDa protein that is not essential for D-ribose high-affinity transport. RbsD is unique as a component of a highaffinit...

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Veröffentlicht in:Florida scientist 2004-07, Vol.67 (3), p.242-245
1. Verfasser: Bouyer, James H.
Format: Artikel
Sprache:eng
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Zusammenfassung:The D-ribose high-affinity transport operon (RbsDACBKR) of Escherichia coli encodes the proteins necessary for high-affinity transport and utilization of D-ribose. rbsD encodes a 15 kDa protein that is not essential for D-ribose high-affinity transport. RbsD is unique as a component of a highaffinity transport system in that it has a TonB box at its amino terminus. Neither RbsD or RbsK are required for D-ribose high-affinity transport, but their potential interaction with each other has not been examined. Characterization of a rbs operon mutant at the TonB box of RbsD implicates the RbsD gene product as a regulator of ribokinase (RbsK) activity.
ISSN:0098-4590