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Scientific article
English

Purification and phosphorylation of the effector protein NopL from Rhizobium sp. NGR234

Contributors

Bartsev, Alexander V.; Boukli Hacene Tani, Nawal Maria; Deakin, William James; Staehelin, Christian; Broughton, William John

Published in

FEBS letters, vol. 554, no. 3, p. 271-274

Publication date

2003

Abstract

Bacterial pathogens use type III secretion systems (TTSSs) to deliver virulence factors into eukaryotic cells. These effectors perturb host-defence responses, especially signal transduction pathways. A functional TTSS was identified in the symbiotic, nitrogen-fixing bacterium Rhizobium sp. NGR234. NopL (formerly y4xL) of NGR234 is a putative symbiotic effector that modulates nodulation in legumes. To test whether NopL could interact with plant proteins, in vitro phosphorylation experiments were performed using recombinant nopL protein purified from Escherichia coli as well as protein extracts from Lotus japonicus and tobacco plants. NopL serves as a substrate for plant protein kinases as well as purified protein kinase A. Phosphorylation of NopL was inhibited by the Ser/Thr kinase inhibitor K252a as well as by PD98059, a mitogen-activated protein (MAP) kinase kinase inhibitor. It thus seems likely that, after delivery into the plant cell, NopL modulates MAP kinase pathways.

Keywords

  • Type III secretion
  • MAP kinase
  • Signal transduction
  • Symbiosis
  • Legume

UNIGE affiliation entities

Citation (ISO format)

BARTSEV, Alexander V. et al. Purification and phosphorylation of the effector protein NopL from Rhizobium sp. NGR234. In: FEBS letters, 2003, vol. 554, n° 3, p. 271–274. doi: 10.1016/s0014-5793(03)01145-1

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Article (Published version)

Identifiers

Journal ISSN

0014-5793
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