A1 Journal article (refereed)
1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain (2021)

Karjalainen, M., Hellman, M., Tossavainen, H., & Permi, P. (2021). 1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain. Biomolecular NMR Assignments, 15(1), 213-217. https://doi.org/10.1007/s12104-021-10008-9

JYU authors or editors

Karjalainen, Mikael
Hellman, Maarit
Aitio, Helena
Permi, Perttu

Publication details

All authors or editors: Karjalainen, Mikael; Hellman, Maarit; Tossavainen, Helena; Permi, Perttu

Journal or series: Biomolecular NMR Assignments

ISSN: 1874-2718

eISSN: 1874-270X

Publication year: 2021

Publication date: 21/01/2021

Volume: 15

Issue number: 1

Pages range: 213-217

Publisher: Springer

Publication country: Netherlands

Publication language: English

DOI: https://doi.org/10.1007/s12104-021-10008-9

Publication open access: Openly available

Publication channel open access: Partially open access channel

Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/73852

Abstract

LEE-encoded effector EspF (EspF) is an effector protein part of enteropathogenic Escherichia coli’s (EPEC’s) arsenal for intestinal infection. This intrinsically disordered protein contains three highly conserved repeats which together compose over half of the protein’s complete amino acid sequence. EPEC uses EspF to hijack host proteins in order to promote infection. In the attack EspF is translocated, together with other effector proteins, to host cell via type III secretion system. Inside host EspF stimulates actin polymerization by interacting with Neural Wiskott-Aldrich syndrome protein (N-WASP), a regulator in actin polymerization machinery. It is presumed that EspF acts by disrupting the autoinhibitory state of N-WASP GTPase binding domain. In this NMR spectroscopy study, we report the 1H, 13C, and 15N resonance assignments for the complex formed by the first 47-residue repeat of EspF and N-WASP GTPase binding domain. These near-complete resonance assignments provide the basis for further studies which aim to characterize structure, interactions, and dynamics between these two proteins in solution.

Keywords: proteins; NMR spectroscopy

Free keywords: EPEC EspF; intrinsically disordered protein; N-WASP; resonance assignments; solution NMR; type III secretion system

Fields of science: