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Plant coilin: structural characteristics and RNA-binding properties.

Makarov V, Rakitina D, Protopopova A, Yaminsky I, Arutiunian A, Love AJ, Taliansky M, Kalinina N - PLoS ONE (2013)

Bottom Line: Atcoilin is able to bind RNA effectively and in a non-specific manner.The interaction with RNA and subsequent multimerization may facilitate coilin's function as a scaffolding protein.A model of the N-terminal domain is also proposed.

View Article: PubMed Central - PubMed

Affiliation: A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, Russia.

ABSTRACT
Cajal bodies (CBs) are dynamic subnuclear compartments involved in the biogenesis of ribonucleoproteins. Coilin is a major structural scaffolding protein necessary for CB formation, composition and activity. The predicted secondary structure of Arabidopsis thaliana coilin (Atcoilin) suggests that the protein is composed of three main domains. Analysis of the physical properties of deletion mutants indicates that Atcoilin might consist of an N-terminal globular domain, a central highly disordered domain and a C-terminal domain containing a presumable Tudor-like structure adjacent to a disordered C terminus. Despite the low homology in amino acid sequences, a similar type of domain organization is likely shared by human and animal coilin proteins and coilin-like proteins of various plant species. Atcoilin is able to bind RNA effectively and in a non-specific manner. This activity is provided by three RNA-binding sites: two sets of basic amino acids in the N-terminal domain and one set in the central domain. Interaction with RNA induces the multimerization of the Atcoilin molecule, a consequence of the structural alterations in the N-terminal domain. The interaction with RNA and subsequent multimerization may facilitate coilin's function as a scaffolding protein. A model of the N-terminal domain is also proposed.

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Structural characteristics of the predicted domains of Atcoilin.(A) Circular dichroism far UV-light spectra of the wt Atcoilin and its isolated domains. (B) Tryptophan fluorescence spectra of the wt Atcoilin and its isolated domains. Fluorescence intensity is given in relative units.
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pone-0053571-g002: Structural characteristics of the predicted domains of Atcoilin.(A) Circular dichroism far UV-light spectra of the wt Atcoilin and its isolated domains. (B) Tryptophan fluorescence spectra of the wt Atcoilin and its isolated domains. Fluorescence intensity is given in relative units.

Mentions: The recombinant proteins corresponding to wild type (wt) Atcoilin and its presumable NOD (1–117 aa residues), IDD (117–350 aa residues) and CTD (350–608 aa residues) domains (Figure 1A) were expressed and purified from E. coli (Figure S2). Their secondary structure was analyzed using a circular dichroism (CD) approach (Figure 2A).


Plant coilin: structural characteristics and RNA-binding properties.

Makarov V, Rakitina D, Protopopova A, Yaminsky I, Arutiunian A, Love AJ, Taliansky M, Kalinina N - PLoS ONE (2013)

Structural characteristics of the predicted domains of Atcoilin.(A) Circular dichroism far UV-light spectra of the wt Atcoilin and its isolated domains. (B) Tryptophan fluorescence spectra of the wt Atcoilin and its isolated domains. Fluorescence intensity is given in relative units.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3539977&req=5

pone-0053571-g002: Structural characteristics of the predicted domains of Atcoilin.(A) Circular dichroism far UV-light spectra of the wt Atcoilin and its isolated domains. (B) Tryptophan fluorescence spectra of the wt Atcoilin and its isolated domains. Fluorescence intensity is given in relative units.
Mentions: The recombinant proteins corresponding to wild type (wt) Atcoilin and its presumable NOD (1–117 aa residues), IDD (117–350 aa residues) and CTD (350–608 aa residues) domains (Figure 1A) were expressed and purified from E. coli (Figure S2). Their secondary structure was analyzed using a circular dichroism (CD) approach (Figure 2A).

Bottom Line: Atcoilin is able to bind RNA effectively and in a non-specific manner.The interaction with RNA and subsequent multimerization may facilitate coilin's function as a scaffolding protein.A model of the N-terminal domain is also proposed.

View Article: PubMed Central - PubMed

Affiliation: A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, Russia.

ABSTRACT
Cajal bodies (CBs) are dynamic subnuclear compartments involved in the biogenesis of ribonucleoproteins. Coilin is a major structural scaffolding protein necessary for CB formation, composition and activity. The predicted secondary structure of Arabidopsis thaliana coilin (Atcoilin) suggests that the protein is composed of three main domains. Analysis of the physical properties of deletion mutants indicates that Atcoilin might consist of an N-terminal globular domain, a central highly disordered domain and a C-terminal domain containing a presumable Tudor-like structure adjacent to a disordered C terminus. Despite the low homology in amino acid sequences, a similar type of domain organization is likely shared by human and animal coilin proteins and coilin-like proteins of various plant species. Atcoilin is able to bind RNA effectively and in a non-specific manner. This activity is provided by three RNA-binding sites: two sets of basic amino acids in the N-terminal domain and one set in the central domain. Interaction with RNA induces the multimerization of the Atcoilin molecule, a consequence of the structural alterations in the N-terminal domain. The interaction with RNA and subsequent multimerization may facilitate coilin's function as a scaffolding protein. A model of the N-terminal domain is also proposed.

Show MeSH