Multiple domains in MtENOD8 protein including the signal peptide target it to the symbiosome Metadata

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Title

  • Main Title Multiple domains in MtENOD8 protein including the signal peptide target it to the symbiosome

Creator

  • Author: Meckfessel, Matthew H.
    Creator Type: Personal
    Creator Info: University of North Texas
  • Author: Blancaflor, Elison B.
    Creator Type: Personal
    Creator Info: Samuel Roberts Noble Foundation
  • Author: Plunkett, Michael
    Creator Type: Personal
    Creator Info: University of North Texas
  • Author: Dong, Qunfeng
    Creator Type: Personal
    Creator Info: University of North Texas
  • Author: Dickstein, Rebecca
    Creator Type: Personal
    Creator Info: University of North Texas

Publisher

  • Name: American Society of Plant Biologists
    Place of Publication: [Rockville, Maryland]

Date

  • Creation: 2012-05

Language

  • English

Description

  • Content Description: Article presenting evidence from GFP fusion experiments that the MtENOD8 protein contains at least three symbiosome targeting domains, including its N-terminal signal peptide (SP).
  • Physical Description: 41 p.

Subject

  • Keyword: plant cells
  • Keyword: proteins
  • Keyword: symbiotic nitrogen fixation
  • Keyword: nodules

Source

  • Journal: Plant Physiology, 2012, Rockville: American Society of Plant Biologists

Citation

  • Publication Title: Plant Physiology
  • Pages: 41
  • Peer Reviewed: True

Collection

  • Name: UNT Scholarly Works
    Code: UNTSW

Institution

  • Name: UNT College of Arts and Sciences
    Code: UNTCAS

Rights

  • Rights Access: public

Resource Type

  • Article

Format

  • Text

Identifier

  • DOI: 10.1104/pp.111.191403
  • Archival Resource Key: ark:/67531/metadc78339

Degree

  • Academic Department: Biological Sciences

Note

  • Display Note: Plant Physiology, May 2012, Vol. 159, pp.299-310, www.plantphysiol.org; © American Society of Plant Biologists.
  • Display Note: Abstract: Symbiotic nitrogen fixation occurs in nodules, specialized organs on the roots of legumes. Within nodules, host plant cells are infected with rhizobia that are encapsulated by a plant-derived membrane forming a novel organelle, the symbiosome. In Medicago truncatula, the symbiosome consists of the symbiosome membrane (SymM), a single rhizobium, and the soluble space between them, called the symbiosome space (Syms). The SymS is enriched with plant-derived proteins, including the MtENOD8 protein. Here, the authors present evidence from GFP fusion experiments that the MtENOD8 protein contains at least three symbiosome targeting domains, including its N-terminal signal peptide (SP). When ectopically expressed in non-nodulated root tissue, the MtENOD8 SP delivers GFP to the vacuole. During the course of nodulation, there is a nodule-specific re-direction MtENOD8-SP-GFP from the vacuole to punctate intermediates and subsequently to symbiosomes, with re-direction of MtENOD8-SP-GFP from the vacuole to punctate intermediates preceding intracellular rhizobial infection. Experiments with Medicago mutants having defects in rhizobial infection and symbiosome development demonstrated that the MtNIP/LATD gene is required for re-direction of the MtENOD8-SP-GFP from the vacuoles to punctate intermediates in nodules. The authors' evidence shows that MtENOD8 has evolved redundant targeting sequences for symbiosome targeting and that intracellular localization of ectopically expressed MtENOD8-SP-GFP is useful as a marker for monitoring the extent of development in mutant nodules.