Dataset Information

Conserved Motifs and Domains in Members of Pospiviroidae.

ABSTRACT: In 1985, Keese and Symons proposed a hypothesis on the sequence and secondary structure of viroids from the family Pospiviroidae: their secondary structure can be subdivided into five structural and functional domains and "viroids have evolved by rearrangement of domains between different viroids infecting the same cell and subsequent mutations within each domain"; this article is one of the most cited in the field of viroids. Employing the pairwise alignment method used by Keese and Symons and in addition to more recent methods, we tried to reproduce the original results and extent them to further members of Pospiviroidae which were unknown in 1985. Indeed, individual members of Pospiviroidae consist of a patchwork of sequence fragments from the family but the lengths of fragments do not point to consistent points of rearrangement, which is in conflict with the original hypothesis of fixed domain borders.

SUBMITTER: Wusthoff KP

PROVIDER: S-EPMC8774013 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature

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Conserved Motifs and Domains in Members of <i>Pospiviroidae</i>.

Wüsthoff Kevin-Phil KP Steger Gerhard G

Cells 20220111 2

In 1985, Keese and Symons proposed a hypothesis on the sequence and secondary structure of viroids from the family <i>Pospiviroidae</i>: their secondary structure can be subdivided into five structural and functional domains and "viroids have evolved by rearrangement of domains between different viroids infecting the same cell and subsequent mutations within each domain"; this article is one of the most cited in the field of viroids. Employing the pairwise alignment method used by Keese and Symo ...[more]

PMID: 35053346

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Project description:Trypanosomatids form a group of protozoa which contain parasites of human, animals and plants. Several of these species cause major human diseases, including Trypanosoma brucei which is the causative agent of human African trypanosomiasis, also called sleeping sickness. These organisms have many highly unusual features including a unique U-insertion/deletion RNA editing process in the single mitochondrion. A key multi-protein complex, called the ∼20S editosome, or editosome, carries out a cascade of essential RNA-modifying reactions and contains a core of 12 different proteins of which six are the interaction proteins A1 to A6. Each of these interaction proteins comprises a C-terminal OB-fold and the smallest interaction protein A6 has been shown to interact with four other editosome OB-folds. Here we report the results of a "linked OB-fold" approach to obtain a view of how multiple OB-folds might interact in the core of the editosome. Constructs with variants of linked domains in 25 expression and co-expression experiments resulted in 13 soluble multi-OB-fold complexes. In several instances, these complexes were more homogeneous in size than those obtained from corresponding unlinked OB-folds. The crystal structure of A3(OB) linked to A6 could be elucidated and confirmed the tight interaction between these two OB domains as seen also in our recent complex of A3(OB) and A6 with nanobodies. In the current crystal structure of A3(OB) linked to A6, hydrophobic side chains reside in well-defined pockets of neighboring OB-fold domains. When analyzing the available crystal structures of editosome OB-folds, it appears that in five instances "Pocket 1" of A1(OB), A3(OB) and A6 is occupied by a hydrophobic side chain from a neighboring protein. In these three different OB-folds, Pocket 1 is formed by two conserved sequence motifs and an invariant arginine. These pockets might play a key role in the assembly or mechanism of the editosome by interacting with hydrophobic side chains from other proteins.

Dataset Information

Conserved Motifs and Domains in Members of Pospiviroidae.

Publications

Conserved Motifs and Domains in Members of <i>Pospiviroidae</i>.

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