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1.
Faraday Discuss ; 169: 195-207, 2014.
Article in English | MEDLINE | ID: mdl-25340471

ABSTRACT

RiboVision is a visualization and analysis tool for the simultaneous display of multiple layers of diverse information on primary (1D), secondary (2D), and three-dimensional (3D) structures of ribosomes. The ribosome is a macromolecular complex containing ribosomal RNA and ribosomal proteins and is a key component of life responsible for the synthesis of proteins in all living organisms. RiboVision is intended for rapid retrieval, analysis, filtering, and display of a variety of ribosomal data. Preloaded information includes 1D, 2D, and 3D structures augmented by base-pairing, base-stacking, and other molecular interactions. RiboVision is preloaded with rRNA secondary structures, rRNA domains and helical structures, phylogeny, crystallographic thermal factors, etc. RiboVision contains structures of ribosomal proteins and a database of their molecular interactions with rRNA. RiboVision contains preloaded structures and data for two bacterial ribosomes (Thermus thermophilus and Escherichia coli), one archaeal ribosome (Haloarcula marismortui), and three eukaryotic ribosomes (Saccharomyces cerevisiae, Drosophila melanogaster, and Homo sapiens). RiboVision revealed several major discrepancies between the 2D and 3D structures of the rRNAs of the small and large subunits (SSU and LSU). Revised structures mapped with a variety of data are available in RiboVision as well as in a public gallery (). RiboVision is designed to allow users to distill complex data quickly and to easily generate publication-quality images of data mapped onto secondary structures. Users can readily import and analyze their own data in the context of other work. This package allows users to import and map data from CSV files directly onto 1D, 2D, and 3D levels of structure. RiboVision has features in rough analogy with web-based map services capable of seamlessly switching the type of data displayed and the resolution or magnification of the display. RiboVision is available at .


Subject(s)
RNA, Ribosomal/chemistry , Ribosomal Proteins/chemistry , Ribosomes/chemistry , Nucleic Acid Conformation , Software
2.
Proc Natl Acad Sci U S A ; 111(28): 10251-6, 2014 Jul 15.
Article in English | MEDLINE | ID: mdl-24982194

ABSTRACT

The origins and evolution of the ribosome, 3-4 billion years ago, remain imprinted in the biochemistry of extant life and in the structure of the ribosome. Processes of ribosomal RNA (rRNA) expansion can be "observed" by comparing 3D rRNA structures of bacteria (small), yeast (medium), and metazoans (large). rRNA size correlates well with species complexity. Differences in ribosomes across species reveal that rRNA expansion segments have been added to rRNAs without perturbing the preexisting core. Here we show that rRNA growth occurs by a limited number of processes that include inserting a branch helix onto a preexisting trunk helix and elongation of a helix. rRNA expansions can leave distinctive atomic resolution fingerprints, which we call "insertion fingerprints." Observation of insertion fingerprints in the ribosomal common core allows identification of probable ancestral expansion segments. Conceptually reversing these expansions allows extrapolation backward in time to generate models of primordial ribosomes. The approach presented here provides insight to the structure of pre-last universal common ancestor rRNAs and the subsequent expansions that shaped the peptidyl transferase center and the conserved core. We infer distinct phases of ribosomal evolution through which ribosomal particles evolve, acquiring coding and translocation, and extending and elaborating the exit tunnel.


Subject(s)
Evolution, Molecular , Phylogeny , RNA, Ribosomal/chemistry , RNA, Ribosomal/genetics , Ribosomes/chemistry , Ribosomes/genetics , Animals , Archaea/chemistry , Archaea/genetics , Bacteria/chemistry , Bacteria/genetics , Fungi/chemistry , Fungi/genetics , Humans , Molecular Structure , RNA, Archaeal/chemistry , RNA, Archaeal/genetics , RNA, Bacterial/chemistry , RNA, Bacterial/genetics , RNA, Fungal/chemistry , RNA, Fungal/genetics , RNA, Protozoan/chemistry , RNA, Protozoan/genetics
3.
PLoS One ; 9(2): e88222, 2014.
Article in English | MEDLINE | ID: mdl-24505437

ABSTRACT

Accurate secondary structures are important for understanding ribosomes, which are extremely large and highly complex. Using 3D structures of ribosomes as input, we have revised and corrected traditional secondary (2°) structures of rRNAs. We identify helices by specific geometric and molecular interaction criteria, not by co-variation. The structural approach allows us to incorporate non-canonical base pairs on parity with Watson-Crick base pairs. The resulting rRNA 2° structures are up-to-date and consistent with three-dimensional structures, and are information-rich. These 2° structures are relatively simple to understand and are amenable to reproduction and modification by end-users. The 2° structures made available here broadly sample the phylogenetic tree and are mapped with a variety of data related to molecular interactions and geometry, phylogeny and evolution. We have generated 2° structures for both large subunit (LSU) 23S/28S and small subunit (SSU) 16S/18S rRNAs of Escherichia coli, Thermus thermophilus, Haloarcula marismortui (LSU rRNA only), Saccharomyces cerevisiae, Drosophila melanogaster, and Homo sapiens. We provide high-resolution editable versions of the 2° structures in several file formats. For the SSU rRNA, the 2° structures use an intuitive representation of the central pseudoknot where base triples are presented as pairs of base pairs. Both LSU and SSU secondary maps are available (http://apollo.chemistry.gatech.edu/RibosomeGallery). Mapping of data onto 2° structures was performed on the RiboVision server (http://apollo.chemistry.gatech.edu/RiboVision).


Subject(s)
Nucleic Acid Conformation , RNA, Ribosomal/chemistry , Animals , Base Pairing , Drosophila melanogaster/chemistry , Drosophila melanogaster/genetics , Haloarcula marismortui/chemistry , Haloarcula marismortui/genetics , Humans , Models, Molecular , Molecular Sequence Data , Phylogeny , RNA, Archaeal/chemistry , RNA, Archaeal/genetics , RNA, Bacterial/chemistry , RNA, Bacterial/genetics , RNA, Fungal/chemistry , RNA, Fungal/genetics , RNA, Ribosomal/genetics , Saccharomyces cerevisiae/chemistry , Saccharomyces cerevisiae/genetics , Thermus thermophilus/chemistry , Thermus thermophilus/genetics
4.
Nucleic Acids Res ; 41(15): 7522-35, 2013 Aug.
Article in English | MEDLINE | ID: mdl-23771137

ABSTRACT

We present a de novo re-determination of the secondary (2°) structure and domain architecture of the 23S and 5S rRNAs, using 3D structures, determined by X-ray diffraction, as input. In the traditional 2° structure, the center of the 23S rRNA is an extended single strand, which in 3D is seen to be compact and double helical. Accurately assigning nucleotides to helices compels a revision of the 23S rRNA 2° structure. Unlike the traditional 2° structure, the revised 2° structure of the 23S rRNA shows architectural similarity with the 16S rRNA. The revised 2° structure also reveals a clear relationship with the 3D structure and is generalizable to rRNAs of other species from all three domains of life. The 2° structure revision required us to reconsider the domain architecture. We partitioned the 23S rRNA into domains through analysis of molecular interactions, calculations of 2D folding propensities and compactness. The best domain model for the 23S rRNA contains seven domains, not six as previously ascribed. Domain 0 forms the core of the 23S rRNA, to which the other six domains are rooted. Editable 2° structures mapped with various data are provided (http://apollo.chemistry.gatech.edu/RibosomeGallery).


Subject(s)
Escherichia coli/genetics , RNA, Bacterial/chemistry , RNA, Ribosomal, 23S/chemistry , RNA, Ribosomal, 5S/chemistry , Base Pairing , Base Sequence , Escherichia coli/chemistry , Evolution, Molecular , Nucleic Acid Conformation , Phylogeny , RNA Folding , RNA Stability , RNA, Bacterial/genetics , Ribosomes/chemistry , Ribosomes/genetics , Structure-Activity Relationship
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