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KMID : 0613820030130050751
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Journal of Life Science
2003 Volume.13 No. 5 p.751 ~ p.755
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Cyclic AMP Receptor Protein Adopts the Highly Stable Conformation at Millimolar cAMP Concentration
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Gang Jong-Back
Choi Young
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Abstract
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Cyclic AMP receptor proteins(CRP) activate many genes in Escherichia coli by binding of cAMP with not fully known mechanism. CRP existed as apo-CRP in the absence of cAMP, CRP:(cAMP)2 at low(micromolar) cAMP concentration, or CRP:(cAMP)4 at high(millimolar) concentration of cAMP. This study is designed to measure the thermal stability of S83G CRP, which substituted glycine for serine at amino acid 83 position, with CD spectrapolarimeter at 222nm by the constant elevation of temperature from 20℃ to 90℃ at 1℃/min. The non-linear regression analysis showed that melting temperatures were 68.4, 72.0, and 82.3℃ for no cAMP, 0.1mM cAMP, and 5mM cAMP, respectively. Result showed the strong thermal stability of CRP by binding of additional cAMP molecules to region between the hinge region and helix-turn-helix(HTH) motif at 5mM cAMP concentration
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KEYWORD
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Cyclic AMP receptor protein(CRP), Molar ellipticity, Thermal stability of protein, Non-linear regression analysis
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