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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Nucleic Acid Structure01:25

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA has a double-helix structure. The...
RNA Structure01:19

RNA Structure

The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA) involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three...
RNA Structure01:23

RNA Structure

Overview
The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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Transcription Attenuation in Prokaryotes02:42

Transcription Attenuation in Prokaryotes

Transcriptional attenuation occurs when RNA transcription is prematurely terminated due to the formation of a terminator mRNA hairpin structure.  Bacteria use these hairpins to regulate the transcription process and control the synthesis of several amino acids including histidine, lysine, threonine, and phenylalanine. Transcription attenuation takes place in the non-coding regions of mRNA.
There are several different mechanisms used to attenuate transcription. In ribosome mediated...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

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Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
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Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

Conformational transitions in human translin enable nucleic acid binding.

Laura Pérez-Cano1, Elad Eliahoo, Keren Lasker

  • 1Joint BSC-IRB research programme in Computational Biology, Barcelona Supercomputing Center (BSC), Jordi Girona 29, Barcelona 08034, Spain, Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel, Blavatnik School of Computer Science, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Tel Aviv 69978, Israel, Bioinformatics Knowledge Unit, The Lorry I. Lokey Interdisciplinary Center for Life Sciences and Engineering, Technion-Israel Institute of Technology, Haifa 32000, Israel and Centre de Biochimie Structurale, INSERM U1054, CNRS UMR 5048, Université Montpellier 1 and 2, F-34090 Montpellier, France.

Nucleic Acids Research
|August 28, 2013
PubMed
Summary

Translin protein exists in multiple forms in solution, with an open octameric state facilitating nucleic acid binding. This structural flexibility explains how translin binds RNA and DNA for cellular functions.

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Published on: September 21, 2017

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Translin is a conserved protein essential for eukaryotic cell function.
  • Its role in nucleic acid binding is unclear due to inaccessible binding sites in known structures.

Purpose of the Study:

  • To elucidate the functional assembly and nucleic acid binding mechanism of translin.
  • To investigate the structural basis of translin's role in RNA metabolism and transport.

Main Methods:

  • Integrative study combining small-angle X-ray scattering (SAXS).
  • Site-directed mutagenesis, biochemical analysis, and computational techniques.
  • Analysis of translin in complex with an RNA oligonucleotide.

Main Results:

  • Translin exhibits significant conformational heterogeneity in solution.
  • A highly populated open octameric state was identified, distinct from the compact state.
  • The internal cavity of the octamer accommodates nucleic acids, with binding residues becoming accessible.

Conclusions:

  • The open octameric state of translin facilitates nucleic acid binding.
  • This provides a structural mechanism for translin's involvement in RNA metabolism and transport.
  • The findings clarify the functional assembly and binding mechanism of this essential protein.