Browse > Article
http://dx.doi.org/10.5352/JLS.2003.13.5.751

Cyclic AMP Receptor Protein Adopts the Highly Stable Conformation at Millimolar cAMP Concentration  

Kang, Jong-Baek (Department of Chemistry, Kyungwon University)
Choi, Young (Department of Chemistry, Kyungwon University)
Publication Information
Journal of Life Science / v.13, no.5, 2003 , pp. 751-755 More about this Journal
Abstract
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$$_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 $20^{\circ]C\; to\; 90^{\circ}C\; at\; 1^{\circ}C/min$. The non-linear regression analysis showed that melting temperatures were 68.4, 72.0, and $82.3^{\circ}C$ 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.
Keywords
Cyclic AMP receptor protein(CRP); Molar ellipticity; Thermal stability of protein; Non-linear regression analysis.;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
연도 인용수 순위
1 Unfolding free energy changes determined by the linear extrapolation method /
[ Santoro,M.M.;D.W.Bolen ] / Biochemistry   DOI   ScienceOn
2 Allosteric regulation of the cAMP receptor protein /
[ Harman,J.G. ] / Biochim Biophys Acta.   DOI   ScienceOn
3 Global conformational changes in allosteric proteins /
[ Heyduk,E.;T.Heyduk;J.C.Lee ] / J. Biol. Chem.
4 Structure of a complex of catabolite gene activator protein and cyclic AMP defined at 2.5 angstrom resolution /
[ Weber,I.T.;T.A.Steitz ] / J. Mol. Biol.   DOI
5 Ligand-induced conformational and structural dynamics changes in Escherichia coli cyclic AMP receptor protein /
[ Dong,A.;J.M.Malecki;L.Lee;J.F.Carpenter;J.C.Lee ] / Biochemistry   DOI   ScienceOn
6 Functional roles of the cyclic AMP-dpendent forms of cyclic AMP receptor protein from Escherichia coli /
[ Mukhopadhyay,J.;R.Sur;P.Parrack ] / FEBS Letters   DOI   ScienceOn
7 Mutagenesis of the cyclic AMP receptor protein of Escherichia Coli: targeting positions of 72 and 82 of cyclic nucleotide binding pocket /
[ Belduz,A.O.;E.J.Lee;J.G.Harman ] / Nucleic Acids Res.   DOI   ScienceOn
8 Structure-function analysis of three cAMP-dependent forms of the cAMP receptor protein /
[ Harman,J.G.;K.McKenney;A.Peterkofsky ] / J. Biol. Chem.
9 Intersubunit association induces unique allosteric dependence of the T127L CRP mutant on pH /
[ Shi,Y.;S.Wang;F.P.Schwarz ] / Biochemistry   DOI   ScienceOn
10 The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer /
[ Passner,J.M.;T.A.Steitz ] / Proc. Natl. Acad. Sci. U. S. A.   DOI   ScienceOn
11 Cyclic adenosine monophosphate receptor: loss of cAMP-dependent DNA binding activity after proteolysis in the presence of cyclic adenosine monophosphate /
[ Krakow,J.S.;I.Patan ] / Proc. Natl. Acad. Sci. U. S. A.   DOI   ScienceOn
12 Study on the structure of cAMP receptor protein(CRP) by temperature change /
[ Joo,J.H.;M.J.Goo;J.B.Gang ] / Kor. J. Life Science   과학기술학회마을
13 Mutagenesis of the cyclic AMP receptor protein of Excherichia Coli: targeting positions of 83, 127 and 128 of cyclic nucleotide binding pocket /
[ Lee,E.J.;J.Glasgow;S.F.Leu;A.O.Beluz;J.G.Harman ] / Nucleic Acid Res.   DOI   ScienceOn
14 Escherichia coli cAMP receptor protein evidence for three protein conformational states with different promoter binding affinities /
[ Heyduk,T.;J.C.Lee ] / Biochemistry   DOI   ScienceOn
15 Transcriptional regulation by cAMP and its receptor protein /
[ Kolb,A.;H.Buc;S.Garges;S.Adhya ] / Ann. Rev. Biochem.   DOI   ScienceOn
16 DNA sequence determinants for binding of the Escherichia coli catabolite gene activator protein /
[ Gunasekera,A.;Y.W.Ebright;R.H.Ebright ] / J. Biol. Chem.