Nature Search

EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences

EF-P plays an important role in overcoming polyproline sequence-induced stalling in bacteria. Here, the authors show that its paralog, EfpL, can also resolve this type of stalling, and also sense cellular metabolic states via lysine acylation.

Alina Sieber
Marina Parr
Jürgen Lassak
ResearchOpen Access02 Dec 2024
Nature Communications

Volume: 15, P: 1-16
A core network in the SARS-CoV-2 nucleocapsid NTD mediates structural integrity and selective RNA-binding

The authors use solution-state NMR and X-ray crystallography to study mutations in the SARS-CoV-2 Nucleocapsid NTD, uncovering a network essential for protein integrity and the selectively of RNA binding.

Karthikeyan Dhamotharan
Sophie M. Korn
Andreas Schlundt
ResearchOpen Access09 Dec 2024
Nature Communications

Volume: 15, P: 1-16
Roquin recognizes a non-canonical hexaloop structure in the 3′-UTR of Ox40

Roquin is an RNA-binding protein that prevents autoimmunity by limiting expression of receptors such as Ox40. Here, the authors identify an RNA structure that they describe as an alternative decay element, and they characterise its interaction with Roquin using structural and biochemical techniques.

Robert Janowski
Gitta A. Heinz
Michael Sattler
ResearchOpen Access24 Mar 2016
Nature Communications

Volume: 7, P: 1-13
The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs

The human RNA exosome contains a nuclear co-factor MTR4, which unwinds structural RNAs and recruits adaptors for different RNA processing and decay pathways. Here the authors uncover new variations of the arch-interacting motif (AIM) in NVL and ZCCHC8 and characterise their interaction with MTR4.

Mahesh Lingaraju
Dennis Johnsen
Elena Conti
ResearchOpen Access29 Jul 2019
Nature Communications

Volume: 10, P: 1-11
Structural basis for RNA recognition in roquin-mediated post-transcriptional gene regulation

Roquin controls T-cell activity through interactions with mRNAs of stimulatory receptors. Structural and functional elucidation of its RNA-binding domain reveals how it interacts with constitutive decay elements in the 3' UTR of its targets to regulate their expression.

Andreas Schlundt
Gitta A Heinz
Michael Sattler
Research13 Jul 2014
Nature Structural & Molecular Biology

Volume: 21, P: 671-678
The preference signature of the SARS-CoV-2 Nucleocapsid NTD for its 5’-genomic RNA elements

SARS-CoV-2 genome turnover is mediated by its N protein, but precise parameters driving the necessary RNA specificity have remained enigmatic. Here, Korn et al. reveal N’s N-terminal domain to distinguish regulatory viral RNA motifs with a preference for transiently folded elements of functional impact.

Sophie Marianne Korn
Karthikeyan Dhamotharan
Andreas Schlundt
ResearchOpen Access07 Jun 2023
Nature Communications

Volume: 14, P: 1-17
Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex

Crystal structures of a localization element of ASH1 mRNA alone, in complex with its nuclear shuttling protein She2p, and in the cytoplasmic complex with She2p and She3p reveal a step-wise maturation pathway.

Franziska Theresia Edelmann
Andreas Schlundt
Dierk Niessing
Research16 Jan 2017
Nature Structural & Molecular Biology

Volume: 24, P: 152-161
Combinatorial recognition of clustered RNA elements by the multidomain RNA-binding protein IMP3

Multidomain RNA-binding proteins recognize specific target sequences through mechanisms that are not well understood. Here the authors present an integrated approach to define the RNA-binding specificity and RNP topology and apply it to the analysis of the prototypical multidomain RNA-binding protein IMP3.

Tim Schneider
Lee-Hsueh Hung
Albrecht Bindereif
ResearchOpen Access22 May 2019
Nature Communications

Volume: 10, P: 1-18
Roquin targets mRNAs in a 3′-UTR-specific manner by different modes of regulation

Roquin targets are known to contain two types of sequence-structure motifs, the constitutive and the alternative decay elements (CDE and ADE). Here, the authors describe a linear Roquin binding element (LBE) also involved in target recognition, and show that Roquin binding affects the translation of a subset of targeted mRNAs.

Katharina Essig
Nina Kronbeck
Vigo Heissmeyer
ResearchOpen Access19 Sept 2018
Nature Communications

Volume: 9, P: 1-17
Structure-function analysis of the DNA-binding domain of a transmembrane transcriptional activator

Andreas Schlundt
Sophie Buchner
Michael Sattler
ResearchOpen Access21 Apr 2017
Scientific Reports

Volume: 7, P: 1-16

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EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences

A core network in the SARS-CoV-2 nucleocapsid NTD mediates structural integrity and selective RNA-binding

Roquin recognizes a non-canonical hexaloop structure in the 3′-UTR of Ox40

The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs

Structural basis for RNA recognition in roquin-mediated post-transcriptional gene regulation

The preference signature of the SARS-CoV-2 Nucleocapsid NTD for its 5’-genomic RNA elements

Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex

Combinatorial recognition of clustered RNA elements by the multidomain RNA-binding protein IMP3

Roquin targets mRNAs in a 3′-UTR-specific manner by different modes of regulation

Structure-function analysis of the DNA-binding domain of a transmembrane transcriptional activator

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