Molecular structures of unbound and transcribing RNA polymerase III

Transcription of genes encoding small structured RNAs such as tRNAs, spliceosomal U6 snRNA and ribosomal 5S RNA is carried out by RNA polymerase III (Pol III), the largest yet structurally least characterized eukaryotic RNA polymerase. The cryo-EM structures of the S. cerevisiae Pol III elongating c...

Full description

Bibliographic Details
Main Authors: Hoffmann, Niklas A., Jakobi, Arjen J., Moreno-Morcillo, Maria, Glatt, Sebastian, Kosinski, Jan, Hagen, Wim J. H., Sachse, Carsten, Müller, Christoph W.
Format: Online
Language:English
Published: 2015
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4681132/
id pubmed-4681132
recordtype oai_dc
spelling pubmed-46811322016-05-25 Molecular structures of unbound and transcribing RNA polymerase III Hoffmann, Niklas A. Jakobi, Arjen J. Moreno-Morcillo, Maria Glatt, Sebastian Kosinski, Jan Hagen, Wim J. H. Sachse, Carsten Müller, Christoph W. Article Transcription of genes encoding small structured RNAs such as tRNAs, spliceosomal U6 snRNA and ribosomal 5S RNA is carried out by RNA polymerase III (Pol III), the largest yet structurally least characterized eukaryotic RNA polymerase. The cryo-EM structures of the S. cerevisiae Pol III elongating complex at 3.9 Å resolution and the apo Pol III enzyme in two different conformations at 4.6 and 4.7 Å resolution, respectively, allow for the first time to build a 17-subunit atomic model of Pol III. The reconstructions reveal the precise orientation of the C82/C34/C31 heterotrimer in close proximity to the stalk. The C53/C37 heterodimer positions residues involved in transcription termination close to the non-template DNA strand. In the apo Pol III structures, the stalk adopts different orientations coupled with closed and open conformations of the clamp. Our results provide novel insights into Pol III-specific transcription and the adaptation of Pol III towards its small transcriptional targets. 2015-11-25 2015-12-10 /pmc/articles/PMC4681132/ /pubmed/26605533 http://dx.doi.org/10.1038/nature16143 Text en Reprints and permissions information is available at www.nature.com/reprints (http://www.nature.com/reprints) . Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Hoffmann, Niklas A.
Jakobi, Arjen J.
Moreno-Morcillo, Maria
Glatt, Sebastian
Kosinski, Jan
Hagen, Wim J. H.
Sachse, Carsten
Müller, Christoph W.
spellingShingle Hoffmann, Niklas A.
Jakobi, Arjen J.
Moreno-Morcillo, Maria
Glatt, Sebastian
Kosinski, Jan
Hagen, Wim J. H.
Sachse, Carsten
Müller, Christoph W.
Molecular structures of unbound and transcribing RNA polymerase III
author_facet Hoffmann, Niklas A.
Jakobi, Arjen J.
Moreno-Morcillo, Maria
Glatt, Sebastian
Kosinski, Jan
Hagen, Wim J. H.
Sachse, Carsten
Müller, Christoph W.
author_sort Hoffmann, Niklas A.
title Molecular structures of unbound and transcribing RNA polymerase III
title_short Molecular structures of unbound and transcribing RNA polymerase III
title_full Molecular structures of unbound and transcribing RNA polymerase III
title_fullStr Molecular structures of unbound and transcribing RNA polymerase III
title_full_unstemmed Molecular structures of unbound and transcribing RNA polymerase III
title_sort molecular structures of unbound and transcribing rna polymerase iii
description Transcription of genes encoding small structured RNAs such as tRNAs, spliceosomal U6 snRNA and ribosomal 5S RNA is carried out by RNA polymerase III (Pol III), the largest yet structurally least characterized eukaryotic RNA polymerase. The cryo-EM structures of the S. cerevisiae Pol III elongating complex at 3.9 Å resolution and the apo Pol III enzyme in two different conformations at 4.6 and 4.7 Å resolution, respectively, allow for the first time to build a 17-subunit atomic model of Pol III. The reconstructions reveal the precise orientation of the C82/C34/C31 heterotrimer in close proximity to the stalk. The C53/C37 heterodimer positions residues involved in transcription termination close to the non-template DNA strand. In the apo Pol III structures, the stalk adopts different orientations coupled with closed and open conformations of the clamp. Our results provide novel insights into Pol III-specific transcription and the adaptation of Pol III towards its small transcriptional targets.
publishDate 2015
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4681132/
_version_ 1613513365826568192