Structural Analysis of a Calmodulin Variant from Rice

Jamshidiha, Mostafa; Ishida, Hiroaki; Sutherland, Cindy; Gifford, Jessica L.; Walsh, Michael P.; Vogel, Hans J.

doi:10.1074/jbc.m113.491076

Cited by 3 publications

(3 citation statements)

References 58 publications

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“…by tuning the time of the tail spent in the cavity. In this way, the tail would control ligand exchange as suggested from earlier work [ 43 , 44 ] and shown here for NCS-1 where tail-effects affected the lifetime of the complex, likely indirectly through modulation of protein stability. The tail lacking one of the critical hydrophobic residues of the motif, from C. elegans , was the only one imposing substantial destabilization.…”

Section: Discussionsupporting

confidence: 58%

“…Nevertheless, as our mutational experiments reveal, the sequence has an influence on tail functionality, although not as pronounced as seen for MutL α (Mlh1-Pms1) mismatch repair (MMR) complex, where scrambling ablated function [ 49 ], but similar to the tail-function in CIB1, where the tail was displaced upon ligand binding [ 44 ]. Finally, it is possible that the tail of NCS-1 may also affect Ca 2+ -binding, as observed for a calmodulin variant from rice [ 43 ], but this remains to be addressed.…”

Section: Discussionmentioning

confidence: 99%

“…Tail-dependent effects have been identified in other calcium-binding proteins. In a calmodulin variant from rice, the disordered C-terminal extension affected both the stability of the apo-state as well as the order of Ca 2+ -ion binding, and the tail was speculated to increase target selectivity [ 43 ]. Similarly, tail-dependent binding specificity was seen for calcium and integrin-binding protein 1 (CIB1) where the C-terminal disordered tail interacted weakly with the ligand-binding hydrophobic channel and was displaced upon ligand binding [ 44 ].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

Staby

Kemplen

Stein

et al. 2020

Cell. Mol. Life Sci.

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Understanding the interplay between sequence, structure and function of proteins has been complicated in recent years by the discovery of intrinsically disordered proteins (IDPs), which perform biological functions in the absence of a well-defined three-dimensional fold. Disordered protein sequences account for roughly 30% of the human proteome and in many proteins, disordered and ordered domains coexist. However, few studies have assessed how either feature affects the properties of the other. In this study, we examine the role of a disordered tail in the overall properties of the two-domain, calcium-sensing protein neuronal calcium sensor 1 (NCS-1). We show that loss of just six of the 190 residues at the flexible C-terminus is sufficient to severely affect stability, dynamics, and folding behavior of both ordered domains. We identify specific hydrophobic contacts mediated by the disordered tail that may be responsible for stabilizing the distal N-terminal domain. Moreover, sequence analyses indicate the presence of an LSL-motif in the tail that acts as a mimic of native ligands critical to the observed order–disorder communication. Removing the disordered tail leads to a shorter life-time of the ligand-bound complex likely originating from the observed destabilization. This close relationship between order and disorder may have important implications for how investigations into mixed systems are designed and opens up a novel avenue of drug targeting exploiting this type of behavior.

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Section: Discussionsupporting

confidence: 58%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

Staby

Kemplen

Stein

et al. 2020

Cell. Mol. Life Sci.

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CaM and CML emergence in the green lineage

Zhu

Dunand

Snedden

et al. 2015

Trends in Plant Science

143

125

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C-terminal extension of calmodulin-like 3 protein from <italic>Oryza sativa</italic> L.: interaction with a high mobility group target protein

Chinpongpanich

Phean-o-pas

Thongchuang

et al. 2015

ABBS

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A large number of calmodulin-like (CML) proteins are present in plants, but there is little detailed information on the functions of these proteins in rice (Oryza sativa L.). Here, the CML3 protein from rice (OsCML3) and its truncated form lacking the C-terminal extension (OsCML3m) were found to exhibit a Ca 2+ -binding property and subsequent conformational change, but the ability to bind the CaM kinase II peptide was only observed for OsCML3m. Changes in their secondary structure upon Ca 2+ -binding measured by circular dichroism revealed that OsCML3m had a higher helical content than OsCML3. Moreover, OsCML3 was mainly localized in the plasma membrane, whereas OsCML3m was found in the nucleus. The rice high mobility group B1 (OsHMGB1) protein was identified as one of the putative OsCML3 target proteins. Bimolecular fluorescence complementation analysis revealed that OsHMGB1 bound OsCML3, OsCML3m or OsCML3s (cysteine to serine mutation at the prenylation site) in the nucleus presumably through the methionine and phenylalaninerich hydrophobic patches, confirming that OsHMGB1 is a target protein in planta. The effect of OsCML3 or OsCML3m on the DNA-binding ability of OsHMGB1 was measured using an electrophoretic mobility shift assay. OsCML3m decreased the level of OsHMGB1 binding to pUC19 doublestranded DNA whereas OsCML3 did not. Taken together, OsCML3 probably provides a mechanism for manipulating the DNA-binding ability of OsHMGB1 in the nucleus and its C-terminal extension provides an intracellular Ca 2+ regulatory switch.

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Structural Analysis of a Calmodulin Variant from Rice

Cited by 3 publications

References 58 publications

Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

CaM and CML emergence in the green lineage

C-terminal extension of calmodulin-like 3 protein from <italic>Oryza sativa</italic> L.: interaction with a high mobility group target protein

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Structural Analysis of a Calmodulin Variant from Rice

Cited by 3 publications

References 58 publications

Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

Disorder in a two-domain neuronal Ca2+-binding protein regulates domain stability and dynamics using ligand mimicry

CaM and CML emergence in the green lineage

C-terminal extension of calmodulin-like 3 protein from &lt;italic&gt;Oryza sativa&lt;/italic&gt; L.: interaction with a high mobility group target protein

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C-terminal extension of calmodulin-like 3 protein from <italic>Oryza sativa</italic> L.: interaction with a high mobility group target protein