Home Life Sciences Homo- and heterotypic interactions between Pss proteins involved in the exopolysaccharide transport system in Rhizobium leguminosarum bv. trifolii
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Homo- and heterotypic interactions between Pss proteins involved in the exopolysaccharide transport system in Rhizobium leguminosarum bv. trifolii

  • Małgorzata Marczak EMAIL logo , Monika Dźwierzyńska and Anna Skorupska
Published/Copyright: February 28, 2013
Biological Chemistry
From the journal Biological Chemistry Volume 394 Issue 4

Abstract

Rhizobium leguminosarum produces large amounts of exopolysaccharide (EPS) that has been shown to be an important determinant of successful nitrogen-fixing symbiosis with legume plants. EPS is assembled in a Wzx/Wzy-dependent manner, and proteins involved in the process are proposed to form a complex that enables coupling the synthesis of EPS subunits with their polymerization and transport. Pss proteins, which are encoded within the chromosomal polysaccharide synthesis cluster of Rhizobium leguminosarum bv. trifolii TA1, were subjected to interaction analysis. PssN was shown to form multimeric complexes in the outer membrane and interact with the extracellular PssO protein and the inner membrane oligomeric PssP co-polymerase. PssO was demonstrated to form oligomers in the presence of the cross-linker. Bacterial two-hybrid analysis showed that PssP interacts with PssL and PssT, counterparts of Gram-negative bacteria Wzx and Wzy proteins. Membrane topology of PssT is discussed in the context of its plausible Wzy-like polymerase activity, interactions with PssP and a possible impact of these interactions on EPS polymerization and chain length determination. The importance of protein-protein and putative protein-polysaccharide interactions in EPS transport is discussed. A topology model for the EPS transport system, with highlights on localization, functions and interactions between the Pss proteins, is proposed.

Keywords: bacterial two-hybrid system; Pss multiprotein complex; Rhizobia; surface polysaccharides; symbiosis
Corresponding author: Małgorzata Marczak, Institute of Microbiology and Biotechnology, Department of Genetics and Microbiology, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, Poland
Received: 2012-3-20
Accepted: 2012-12-4
Published Online: 2013-02-28
Published in Print: 2013-04-01

©2013 by Walter de Gruyter Berlin Boston

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  17. Homo- and heterotypic interactions between Pss proteins involved in the exopolysaccharide transport system in Rhizobium leguminosarum bv. trifolii
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https://doi.org/10.1515/hsz-2012-0161
Keywords for this article
bacterial two-hybrid system; Pss multiprotein complex; Rhizobia; surface polysaccharides; symbiosis

Articles in the same Issue

  1. Masthead
  2. Masthead
  3. Guest Editorial
  4. Highlight: sensing hypoxia in the cell and the organism
  5. Highlight: Sensing Hypoxia in the Cell and the Organism
  6. Hypoxia-inducible factor prolyl 4-hydroxylases: common and specific roles
  7. The regulation, localization, and functions of oxygen-sensing prolyl hydroxylase PHD3
  8. Deciphering the emerging role of SUMO conjugation in the hypoxia-signaling cascade
  9. Hypoxia, the HIF pathway and neutrophilic inflammatory responses
  10. Hydroxylase-dependent regulation of the NF-κB pathway
  11. Role of hypoxia inducible factor-1α for interferon synthesis in mouse dendritic cells
  12. Pan-genomic binding of hypoxia-inducible transcription factors
  13. HIF mediated and DNA damage independent histone H2AX phosphorylation in chronic hypoxia
  14. Noninvasive assessment of hypoxia with 3-[18F]-fluoro-1-(2-nitro-1-imidazolyl)-2-propanol ([18F]-FMISO): a PET study in two experimental models of human glioma
  15. Research Articles/Short Communications
  16. Protein Structure and Function
  17. Homo- and heterotypic interactions between Pss proteins involved in the exopolysaccharide transport system in Rhizobium leguminosarum bv. trifolii
  18. Proteolysis
  19. Combination of quercetin and tannic acid in inhibiting 26S proteasome affects S5a and 20S expression, and accumulation of ubiquitin resulted in apoptosis in cancer chemoprevention
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