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Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers

Hantaan virus polymerase is a central enzyme that performs hantavirus genome replication and transcription. Here, the authors unveil the structure of the full-length Hantaan virus polymerase in monomeric, dimeric and hexameric apo forms, revealing the multimerization capability of this enzyme.

Quentin Durieux Trouilleton
Dominique Housset
Hélène Malet
ResearchOpen Access13 Mar 2024
Nature Communications

Volume: 15, P: 1-17
Structures of active Hantaan virus polymerase uncover the mechanisms of Hantaviridae genome replication

Hantaan virus is a lifethreatening Bunyavirus. Here the authors determine the cryoelectron microscopy structure of its polymerase, a central enzyme involved in viral genome replication. Structures combined with in vitro activity decipher at high resolution the molecular mechanisms of the replication cycle.

Quentin Durieux Trouilleton
Sergio Barata-García
Hélène Malet
ResearchOpen Access23 May 2023
Nature Communications

Volume: 14, P: 1-15
Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes

RNA-dependent RNA polymerases from segmented negative stranded RNA viruses catalyze genome replication and viral transcription. Here, the authors present the cryo-EM structure of full-length La Crosse virus polymerase and structurally characterize the pre-initiation and elongation states, which is of interest for the development of polymerase inhibitors.

Benoît Arragain
Grégory Effantin
Hélène Malet
ResearchOpen Access17 Jul 2020
Nature Communications

Volume: 11, P: 1-13
Structural snapshots of La Crosse virus polymerase reveal the mechanisms underlying Peribunyaviridae replication and transcription

La Crosse is a human life threatening virus belonging to the Bunyavirales order. The structure of its polymerase solved in seven key active states by cryo-electron microscopy reveals the molecular mechanisms of viral RNA replication and transcription.

Benoît Arragain
Quentin Durieux Trouilleton
Hélène Malet
ResearchOpen Access16 Feb 2022
Nature Communications

Volume: 13, P: 1-16
Structural insight into cap-snatching and RNA synthesis by influenza polymerase

Atomic resolution crystal structures of influenza A and B polymerases are presented; comparison of these structures provides mechanistic insight into influenza polymerase functions, explaining the processes of cap-snatching and cap-dependent priming, which are unique to segmented negative-strand RNA viruses.

Stefan Reich
Delphine Guilligay
Stephen Cusack
Research19 Nov 2014
Nature

Volume: 516, P: 361-366
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ

HtrA proteins have chaperone and protease activities, but how they bind and fold their substrates is poorly understood. New cryo-EM analyses of a protease-defective bacterial DegQ mutant in complex with several different substrates provide a structural model of HtrA proteins in their chaperone mode.

Hélène Malet
Flavia Canellas
Helen R Saibil
Research15 Jan 2012
Nature Structural & Molecular Biology

Volume: 19, P: 152-157
Basal foot MTOC organizes pillar MTs required for coordination of beating cilia

Coordinated beating of motile cilia is important to clear mucus from the airway. Here, Clare et al. show that galectin-3 at the base of motile cilia in the trachea is important for connecting cortical microtubules to the basal body, and subsequent organization and coordination of beating cilia.

Daniel K. Clare
Jérémy Magescas
Delphine Delacour
Research12 Sept 2014
Nature Communications

Volume: 5, P: 1-9
Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex

Jessop, Arragain et al characterise the structure of the E.coli AAA+ ATPase RavA alone and in complex with the acid stress inducible lysine decarboxylase LdcI. Their results reveal two co-existing structural states of RavA and provide insights into the ATPase cycle that might be generalizable to other AAA+ ATPases of clade 7.

Matthew Jessop
Benoit Arragain
Irina Gutsche
ResearchOpen Access28 Jan 2020
Communications Biology

Volume: 3, P: 1-14
Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small protein

Francesca Coscia
Leandro F. Estrozi
Carlo Petosa
ResearchOpen Access03 Aug 2016
Scientific Reports

Volume: 6, P: 1-11
Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA

Eaazhisai Kandiah
Diego Carriel
Irina Gutsche
ResearchOpen Access15 Apr 2016
Scientific Reports

Volume: 6, P: 1-12

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Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers

Structures of active Hantaan virus polymerase uncover the mechanisms of Hantaviridae genome replication

Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes

Structural snapshots of La Crosse virus polymerase reveal the mechanisms underlying Peribunyaviridae replication and transcription

Structural insight into cap-snatching and RNA synthesis by influenza polymerase

Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ

Basal foot MTOC organizes pillar MTs required for coordination of beating cilia

Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex

Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small protein

Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA

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