Interaction of calmodulin with the phosphofructokinase target sequence

Ca 4 · calmodulin (Ca 4 · CaM) inhibits the glycolytic enzyme phosphofructokinase, by preventing formation of its active tetramer. Fluorescence titrations show that the affinity of complex formation of Ca 4 · CaM with the key 21-residue target peptide increases 1000-fold from pH 9.0 to 4.8, suggesti...

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Bibliographic Details
Published in:	FEBS letters Vol. 577; no. 1; pp. 284 - 288
Main Authors:	Martin, Stephen R., Biekofsky, Rodolfo R., Skinner, Murray A., Guerrini, Remo, Salvadori, Severo, Feeney, James, Bayley, Peter M.
Format:	Journal Article
Language:	English
Published:	England Elsevier B.V 05-11-2004
Subjects:	Animals Calcium - metabolism Calmodulin Calmodulin - metabolism CaM, calmodulin Drosophila melanogaster Fluorescence Histidine Hydrogen-Ion Concentration Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Other peptides, see PFK peptides , P1–26 KLRGRSFMNNWEVYKLLAHIRPPAPK, (rabbit muscle PFK, residues 371–396) and the corresponding peptides P9–21, P1–21 and P1–21(E12Q) sequences PFK, 6-phosphofructokinase Phosphofructokinase Phosphofructokinases - chemistry Phosphofructokinases - metabolism Protein Binding Recombinant Proteins - metabolism Spectrometry, Fluorescence Target sequences PFK, 6-phosphofructokinase Histidine PFK peptides , P 1–26 KLRGRSFMNNWEVYKLLAHIRPPAPK, (rabbit muscle PFK, residues 371–396) and the corresponding peptides P 9–21, P 1–21 and P 1–21(E12Q) sequences Fluorescence CaM, calmodulin Nuclear magnetic resonance Target sequences Other peptides, see Calmodulin Phosphofructokinase
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Summary:	Ca 4 · calmodulin (Ca 4 · CaM) inhibits the glycolytic enzyme phosphofructokinase, by preventing formation of its active tetramer. Fluorescence titrations show that the affinity of complex formation of Ca 4 · CaM with the key 21-residue target peptide increases 1000-fold from pH 9.0 to 4.8, suggesting the involvement of histidine and carboxylic acid residues. 1H NMR pH titration indicates a marked increase in p K a of the peptide histidine on complex formation and HSQC spectra show related pH-dependent changes in the conformation of the complex. This unusually strong sensitivity of a CaM–target complex to pH suggests a potential functional role for Ca 4 · CaM in regulation of the glycolytic pathway.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2004.10.023