Biochemical and biophysical characterization of a plant calmodulin: Role of the N- and C-lobes in calcium binding, conformational change, and target interaction
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- 作者：Alessandra Astegnoa ; alessandra.astegno@univr.it" class="auth_mail" title="E-mail the corresponding author ; Valentina La Verdea ; Valerio Marinob ; Daniele Dell'Orcob ; Paola Dominicia
- 关键词：Ca2 ; + ; ; calcium ; CaM ; calmodulin ; AtCaM1 ; Arabidopsis calmodulin isoform 1 ; B12Q ; AtCaM1 EE32-68QQ mutant ; B34Q ; AtCaM1 EE105-141QQ mutant ; GAD ; glutamate decarboxylase ; GAD1 ; Arabidopsis glutamate decarboxylase isoform 1 ; CaMBD ; calmodulin binding domain ; GAD1p ; GAD1 peptide ; ITC ; isothermal titration calorimetry ; MD ; molecular dynamics ; EGTA ; Ethylene glycol-bis(2-aminoethylether)-N ; N ; N&prime ; N&prime ; -tetraacetic acid ; Kd ; dissociation constant ; Rs ; Stokes radius ; SEC ; size exclusio
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：March 2016
- 年：2016
- 卷：1864
- 期：3
- 页码：297-307
- 全文大小：1316 K
文摘
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Plant GAD is activated in response to abiotic stress via association with CaM.
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AtCaM1 binds four Ca2 + ions with an apparent Kd of 20.0 ± 1.2 μM.
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The C-lobe of AtCaM1 has a ~ 6-fold stronger Ca2 + binding affinity than the N-lobe.
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N- and C-lobes of AtCaM1 differ in their conformational dynamics.
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Only intact AtCaM1, and not the form with perturbed N- or C-lobe, is able to fully activate GAD1.