Publications by authors named "M Krzymowska"

Virulence of many gram-negative bacteria relies upon delivery of type three effectors into host cells. To pass through the conduit of secretion machinery the effectors need to acquire an extended conformation, and in many bacterial species specific chaperones assist in this process. In plant pathogenic bacterium Pseudomonas syringae, secretion of only few effectors requires the function of chaperones.

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Article Synopsis
  • HopQ1, a type three effector, recruits plant 14-3-3 proteins through phosphorylation, impacting its stability and location in the cell.
  • Mass spectrometry identified phosphorylation at serine 51 and 14-3-3 binding motifs, with both sites contributing to forming a complex that limits HopQ1's movement into the nucleus.
  • The study suggests that while HopQ1 has a potential nuclear translocation signal, its interaction with 14-3-3 proteins actually slows its nuclear import, illustrating a balance in its localization within the cell.
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In Arabidopsis, a dry stigma surface enables a gradual hydration of pollen grains by a controlled release of water. Occasionally the grains may be exposed to extreme precipitations that cause rapid water influx and swelling, eventually leading to pollen membrane rupture. In metazoans, calcium- and phospholipid-binding proteins, referred to as annexins, participate in the repair of plasma membrane damages.

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The molecular chaperone HSP90 facilitates the folding of several client proteins, including innate immune receptors and protein kinases. HSP90 is an essential component of plant and animal immunity, yet pathogenic strategies that directly target the chaperone have not been described. Here, we identify the HopBF1 family of bacterial effectors as eukaryotic-specific HSP90 protein kinases.

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Background: Pollen development is a strictly controlled post-meiotic process during which microspores differentiate into microgametophytes and profound structural and functional changes occur in organelles. Annexin 5 is a calcium- and lipid-binding protein that is highly expressed in pollen grains and regulates pollen development and physiology. To gain further insights into the role of ANN5 in Arabidopsis development, we performed detailed phenotypic characterization of Arabidopsis plants with modified ANN5 levels.

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