Literature DB >> 19954189

Variations at the semiconserved glycine in the IQ domain consensus sequence have a major impact on Ca2+-dependent switching in calmodulin-IQ domain complexes.

D J Black1, Anthony Persechini.   

Abstract

We have replaced the semiconserved Gly in the IQ domain consensus sequence with Ala, Arg, or Met in a reference sequence and determined how this affects its complexes with calmodulin. The K(d) for the Ca(2+)-free reference complex is 2.4 +/- 0.3 microM. The Ala and Arg replacements increase this to 5.4 +/- 0.4 and 6.2 +/- 0.5 microM, while the Met increases it to 26.4 +/- 2.5 microM. When Ca(2+) is bound to both calmodulin lobes, the K(d) for the reference complex is not significantly affected, but the K(d) for the Ala variant decreases to 0.9 +/- 0.04 microM, and the values for the Arg and Met variants decrease to 0.4 +/- 0.03 microM. Using mutant calmodulins, we defined the effect of Ca(2+) binding to each lobe, with the C-terminal preceding the N-terminal (C-->N) or vice versa (N-->C). In the C-->N order the first step increases the reference K(d) approximately 5-fold, while it decreases the values for the variants approximately 2- to approximately 10-fold. The second step decreases the K(d) values for the all of the complexes approximately 5-fold, suggesting that the N-terminal lobe does not interact with the semiconserved position after the first step. In the N-->C order the first step increases the K(d) values for the reference complex and Met and Ala variants approximately 15- to approximately 200-fold but does not affect the value for the Arg variant. The second step decreases the K(d) values for the reference and Arg variant approximately 10- and approximately 15-fold and the Ala and Met variants approximately 2000-fold. Thus, both steps in the N-->C order are sensitive to variations at the semiconserved position, while only the first is in the C-->N order. Due to energy coupling, this order is followed under equilibrium conditions.

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Year:  2010        PMID: 19954189      PMCID: PMC3105379          DOI: 10.1021/bi901695p

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  23 in total

1.  Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications.

Authors:  Mohammed Terrak; Guanming Wu; Walter F Stafford; Renne C Lu; Roberto Dominguez
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2.  Apocalmodulin and Ca2+ calmodulin-binding sites on the CaV1.2 channel.

Authors:  Wei Tang; D Brent Halling; D J Black; Patricia Pate; Jia-Zheng Zhang; Steen Pedersen; Ruth A Altschuld; Susan L Hamilton
Journal:  Biophys J       Date:  2003-09       Impact factor: 4.033

Review 3.  Calmodulin signaling via the IQ motif.

Authors:  Martin Bähler; Allen Rhoads
Journal:  FEBS Lett       Date:  2002-02-20       Impact factor: 4.124

4.  Structure of calmodulin refined at 2.2 A resolution.

Authors:  Y S Babu; C E Bugg; W J Cook
Journal:  J Mol Biol       Date:  1988-11-05       Impact factor: 5.469

5.  The identification and characterization of a noncontinuous calmodulin-binding site in noninactivating voltage-dependent KCNQ potassium channels.

Authors:  Eva Yus-Najera; Irene Santana-Castro; Alvaro Villarroel
Journal:  J Biol Chem       Date:  2002-05-24       Impact factor: 5.157

Review 6.  Calmodulin is a limiting factor in the cell.

Authors:  Anthony Persechini; Paul M Stemmer
Journal:  Trends Cardiovasc Med       Date:  2002-01       Impact factor: 6.677

7.  Regulation of the RYR1 and RYR2 Ca2+ release channel isoforms by Ca2+-insensitive mutants of calmodulin.

Authors:  Bradley R Fruen; D J Black; Rachel A Bloomquist; Jennifer M Bardy; J David Johnson; Charles F Louis; Edward M Balog
Journal:  Biochemistry       Date:  2003-03-11       Impact factor: 3.162

8.  The central helix of calmodulin functions as a flexible tether.

Authors:  A Persechini; R H Kretsinger
Journal:  J Biol Chem       Date:  1988-09-05       Impact factor: 5.157

9.  The IQ domains in neuromodulin and PEP19 represent two major functional classes.

Authors:  D J Black; David LaMartina; Anthony Persechini
Journal:  Biochemistry       Date:  2009-12-15       Impact factor: 3.162

10.  HMM Logos for visualization of protein families.

Authors:  Benjamin Schuster-Böckler; Jörg Schultz; Sven Rahmann
Journal:  BMC Bioinformatics       Date:  2004-01-21       Impact factor: 3.169

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  3 in total

1.  Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaV1.2.

Authors:  Liam Hovey; C Andrew Fowler; Ryan Mahling; Zesen Lin; Mark Stephen Miller; Dagan C Marx; Jesse B Yoder; Elaine H Kim; Kristin M Tefft; Brett C Waite; Michael D Feldkamp; Liping Yu; Madeline A Shea
Journal:  Biophys Chem       Date:  2017-03-09       Impact factor: 2.352

2.  Kinetic analysis reveals differences in the binding mechanism of calmodulin and calmodulin-like protein to the IQ motifs of myosin-10.

Authors:  Ariel J Caride; Richard D Bennett; Emanuel E Strehler
Journal:  Biochemistry       Date:  2010-09-21       Impact factor: 3.162

3.  Pivoting between calmodulin lobes triggered by calcium in the Kv7.2/calmodulin complex.

Authors:  Alessandro Alaimo; Araitz Alberdi; Carolina Gomis-Perez; Juncal Fernández-Orth; Ganeko Bernardo-Seisdedos; Covadonga Malo; Oscar Millet; Pilar Areso; Alvaro Villarroel
Journal:  PLoS One       Date:  2014-01-28       Impact factor: 3.240

  3 in total

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