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KMID : 0578319960060020133
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Molecules and Cells
1996 Volume.6 No. 2 p.133 ~ p.138
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Tactic Interaction of ribose-binding Protein with the membrane Receptor Trg
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Kim Chang-Hoon
Jung Kwang-Hwan
Eym Yong-Bin
Park Chan-Kyu
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Abstract
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To investigate the interaction between ribose-binding protein (RBP) and Trg chemosen-sory transducer, we have isolated suppressor mutations in RBP for the trg-8 mutation that causes a specific defect in chemotactic response to ribose. In addition, nonchemotactic mutations of RBP were isolated. The mutations were characterized by measuring binding affinity, uptake rate, and chemotactic response in capillary. They exhibit altered responses to ribose, while one of them show additional transport defects. In order to quantitatively monitor the interaction of RBP with Trg, an assay using the chimeric receptor Trzl (Baumgartner et al., 1994) was performed, indicating changes of the mutant RBP in their affinities to the receptor. The results imply that the interactive surface on RBP involves the regions around the binding cleft including residues 65 and 192 on the three-di-mensional structure of RBP.
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KEYWORD
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