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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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Amino acid sequence analysis and predicted domain organization of Arabidopsis thalianacoilin. (A) Schematic representation of functional sites and regions that have been identified within the coilin protein molecule. (B) The predicted domain organization of Arabidopsis thaliana coilin, as elucidated by the bioinformatic tools FoldIndex and DISOPRED.
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pone-0053571-g001: Amino acid sequence analysis and predicted domain organization of Arabidopsis thalianacoilin. (A) Schematic representation of functional sites and regions that have been identified within the coilin protein molecule. (B) The predicted domain organization of Arabidopsis thaliana coilin, as elucidated by the bioinformatic tools FoldIndex and DISOPRED.

Mentions: The schematic representation of coilin from Arabidopsis thaliana (NM_101173.4; GI:42562030), Atcoilin, a 608-amino acid protein [7] which shares functional and structural characteristics with vertebrate (human) coilin, is shown in Figure 1A. As demonstrated by [7], there are two regions with high homology between the vertebrate and plant coilins: the N-terminal 100 amino acid residues, and the C-terminal 100 amino acid region encompassing a Tudor-like domain (corresponding to the C-terminal residues 460–560 and 410–510 of human coilin and Atcoilin respectively). The N-terminal region is suggested to be responsible for the self-association of the protein [18]. Similar to human coilin, two NLSs are predicted in the central part of the protein [7].


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)

Amino acid sequence analysis and predicted domain organization of Arabidopsis thalianacoilin. (A) Schematic representation of functional sites and regions that have been identified within the coilin protein molecule. (B) The predicted domain organization of Arabidopsis thaliana coilin, as elucidated by the bioinformatic tools FoldIndex and DISOPRED.
© Copyright Policy
Related In: Results  -  Collection

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

pone-0053571-g001: Amino acid sequence analysis and predicted domain organization of Arabidopsis thalianacoilin. (A) Schematic representation of functional sites and regions that have been identified within the coilin protein molecule. (B) The predicted domain organization of Arabidopsis thaliana coilin, as elucidated by the bioinformatic tools FoldIndex and DISOPRED.
Mentions: The schematic representation of coilin from Arabidopsis thaliana (NM_101173.4; GI:42562030), Atcoilin, a 608-amino acid protein [7] which shares functional and structural characteristics with vertebrate (human) coilin, is shown in Figure 1A. As demonstrated by [7], there are two regions with high homology between the vertebrate and plant coilins: the N-terminal 100 amino acid residues, and the C-terminal 100 amino acid region encompassing a Tudor-like domain (corresponding to the C-terminal residues 460–560 and 410–510 of human coilin and Atcoilin respectively). The N-terminal region is suggested to be responsible for the self-association of the protein [18]. Similar to human coilin, two NLSs are predicted in the central part of the protein [7].

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