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RNA Structure01:19

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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.
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Nanomanipulation of Single RNA Molecules by Optical Tweezers
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An alternative RNA polymerase I structure reveals a dimer hinge.

Dirk Kostrewa1, Claus-D Kuhn2, Christoph Engel3

  • 1Gene Center Munich and Department of Biochemistry, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.

Acta Crystallographica. Section D, Biological Crystallography
|September 2, 2015
PubMed
Summary

RNA polymerase I (Pol I) structures reveal how the expander and connector influence enzyme dimerization and active-center conformation. This provides new insights into ribosomal RNA precursor synthesis in eukaryotic cells.

Keywords:
RNA polymerase Iconnectordimerhinge

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • RNA polymerase I (Pol I) is a crucial 14-subunit enzyme responsible for synthesizing ribosomal RNA (rRNA) precursors in eukaryotes.
  • Previous structural studies identified an 'expander' and a 'connector' in Pol I, influencing its active-center and dimerization.

Purpose of the Study:

  • To investigate the structural role of the 'expander' and 'connector' in RNA polymerase I (Pol I) dimerization and function.
  • To characterize an alternative crystal form of Pol I and its implications for enzyme structure.

Main Methods:

  • X-ray crystallography to solve an alternative crystal form of Pol I.
  • Molecular replacement using a previously determined Pol I structure.
  • Structural comparison of the two Pol I forms.

Main Results:

  • An alternative Pol I structure was determined, lacking the 'expander' but retaining an expanded active-center cleft.
  • Neighboring Pol I monomers formed a homodimer with a distinct relative orientation compared to previous findings.
  • The 'connector' element was confirmed to act as a hinge mediating Pol I dimerization.

Conclusions:

  • The 'expander' is not essential for maintaining an expanded active-center cleft in Pol I.
  • The 'connector' plays a critical role in Pol I dimerization, acting as a flexible hinge.
  • Structural plasticity of Pol I influences rRNA precursor synthesis regulation.