Aptly named aptamers display their aptitude

Article Abstract:

ATP-aptamers are RNAs that exhibit ATP-binding ability similar to proteins, and can bind proteins, amino acids, nucleotides and vitamin cofactors. A part of the ATP-aptamer's structure, in which ATP can fit into a nucleotide-binding pocket, is identical to the GNRA tetraloop. The GNRA loop sequence has unusual stability due to the formation of a G-A base pair and stacking interaction. However, cell structure has the bound adenosine nucleotide occupying the position of A residue. ATP-aptamers prove the ability of primordial RNAs to perform like proteins.

Analysis, RNA, Adenosine triphosphate, ATP

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An assembly landscape for the 30s ribosomal subunit

Article Abstract:

The ribosome, which carries out protein synthesis, is the preeminent model system for biophysical analysis of large RNA protein complexes and self assembling macromolecular machines drive fundamental cellular processes including transcription translation DNA replication and cellular transport. The pathway proceeding through a global rate limiting conformational change gives way to one in which the assembly of the complex traverses a landscape dotted with various local conformational transitions.

United States, Science & research, Research, Protein synthesis, Genetic transcription, Transcription (Genetics), Protein biosynthesis, Ribosomal proteins

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Small subunit, big science

Article Abstract:

Issues are presented concerning the structure and function of ribosomes. The protein production capabilities of ribosomes and their use as messenger RNA decoding sites are discussed.

Cells (Biology), Cells, Ribosomes

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