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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Putkey, John A. Goldsmith, Michael Kleerekoper, Quinn K. Brewer, Kari J. Gaertner, Tara R. Kubota, Yoshihisa Waxham, M. Neal |
| Description | Author Affiliation: Putkey JA ( Department of Biochemistry and Molecular Biology, University of Texas, Houston Medical School, Houston, TX 77030, USA. john.putkey@uth.tmc.edu) |
| Abstract | The small IQ motif proteins PEP-19 (62 amino acids) and RC3 (78 amino acids) greatly accelerate the rates of Ca(2+) binding to sites III and IV in the C-domain of calmodulin (CaM). We show here that PEP-19 decreases the degree of cooperativity of Ca(2+) binding to sites III and IV, and we present a model showing that this could increase Ca(2+) binding rate constants. Comparative sequence analysis showed that residues 28 to 58 from PEP-19 are conserved in other proteins. This region includes the IQ motif (amino acids 39-62), and an adjacent acidic cluster of amino acids (amino acids 28-40). A synthetic peptide spanning residues 28-62 faithfully mimics intact PEP-19 with respect to increasing the rates of Ca(2+) association and dissociation, as well as binding preferentially to the C-domain of CaM. In contrast, a peptide encoding only the core IQ motif does not modulate Ca(2+) binding, and binds to multiple sites on CaM. A peptide that includes only the acidic region does not bind to CaM. These results show that PEP-19 has a novel acidic/IQ CaM regulatory motif in which the IQ sequence provides a targeting function that allows binding of PEP-19 to CaM, whereas the acidic residues modify the nature of this interaction, and are essential for modulating Ca(2+) binding to the C-domain of CaM. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 3 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-01-18 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Calmodulin Metabolism Peptides Amides Amino Acid Motifs Amino Acid Sequence Calcium Chemistry Consensus Sequence Kinetics Molecular Sequence Data Protein Binding Protein Conformation Protein Interaction Mapping Sequence Alignment Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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