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Structure paper

TitleStructural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 1729, Year 2023
Publish dateMar 28, 2023
AuthorsPhong Quoc Nguyen / Sonia Huecas / Amna Asif-Laidin / Adrián Plaza-Pegueroles / Beatrice Capuzzi / Noé Palmic / Christine Conesa / Joël Acker / Juan Reguera / Pascale Lesage / Carlos Fernández-Tornero /
PubMed AbstractThe yeast Ty1 retrotransposon integrates upstream of genes transcribed by RNA polymerase III (Pol III). Specificity of integration is mediated by an interaction between the Ty1 integrase (IN1) and ...The yeast Ty1 retrotransposon integrates upstream of genes transcribed by RNA polymerase III (Pol III). Specificity of integration is mediated by an interaction between the Ty1 integrase (IN1) and Pol III, currently uncharacterized at the atomic level. We report cryo-EM structures of Pol III in complex with IN1, revealing a 16-residue segment at the IN1 C-terminus that contacts Pol III subunits AC40 and AC19, an interaction that we validate by in vivo mutational analysis. Binding to IN1 associates with allosteric changes in Pol III that may affect its transcriptional activity. The C-terminal domain of subunit C11, involved in RNA cleavage, inserts into the Pol III funnel pore, providing evidence for a two-metal mechanism during RNA cleavage. Additionally, ordering next to C11 of an N-terminal portion from subunit C53 may explain the connection between these subunits during termination and reinitiation. Deletion of the C53 N-terminal region leads to reduced chromatin association of Pol III and IN1, and a major fall in Ty1 integration events. Our data support a model in which IN1 binding induces a Pol III configuration that may favor its retention on chromatin, thereby improving the likelihood of Ty1 integration.
External linksNat Commun / PubMed:36977686 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.2 Å
Structure data

14421

7z0h

EMDB-14421, PDB-7z0h:
Structure of yeast RNA Polymerase III-Ty1 integrase complex at 2.6 A (focus subunit AC40).
Method: EM (single particle) / Resolution: 2.6 Å

14468

7z2z

EMDB-14468, PDB-7z2z:
Structure of yeast RNA Polymerase III-DNA-Ty1 integrase complex (Pol III-DNA-IN1) at 3.1 A
Method: EM (single particle) / Resolution: 3.07 Å

14469

7z30

EMDB-14469, PDB-7z30:
Structure of yeast RNA Polymerase III-Ty1 integrase complex at 2.9 A (focus subunit C11 terminal Zn-ribbon in the funnel pore).
Method: EM (single particle) / Resolution: 2.9 Å

14470

7z31

EMDB-14470, PDB-7z31:
Structure of yeast RNA Polymerase III-Ty1 integrase complex at 2.7 A (focus subunit C11, no C11 C-terminal Zn-ribbon in the funnel pore).
Method: EM (single particle) / Resolution: 2.76 Å

16299

8bws

EMDB-16299, PDB-8bws:
Structure of yeast RNA Polymerase III elongation complex at 3.3 A
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-4QM:
(3R,5S,7R,8R,9S,10S,12S,13R,14S,17R)-10,13-dimethyl-17-[(2R)-pentan-2-yl]-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthrene-3,7,12-triol

Source
  • saccharomyces cerevisiae s288c (yeast)
KeywordsTRANSCRIPTION / targeted DNA integration / Ty1 retrotransposon / Ty1 integrase / RNA 19 polymerase III

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