Search results for: DKSA

• Multicopy Suppressor Analysis of Strains Lacking Cytoplasmic Peptidyl-Prolyl cis/trans Isomerases Identifies Three New PPIase Activities in Escherichia coli That Includes the DksA Transcription Factor

  Publication

  • P. Wojtkiewicz
  • D. Biernacka
  • P. Gorzelak
  • A. Stupak
  • G. Klein-Raina
  • S. Raina

  - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES - Year 2020

  Consistent with a role in catalyzing rate-limiting step of protein folding, removal of genes encoding cytoplasmic protein folding catalysts belonging to the family of peptidyl-prolyl cis/trans isomerases (PPIs) in Escherichia coli confers conditional lethality. To address the molecular basis of the essentiality of PPIs, a multicopy suppressor approach revealed that overexpression of genes encoding chaperones (DnaK/J and GroL/S),...

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• Agnieszka Potęga dr inż.

  People

  Department of Pharmaceutical Technology and Biochemistry

• A new factor LapD is required for the regulation of LpxC amounts and lipopolysaccharide trafficking

  Publication

  • A. Wieczorek
  • A. Sendobra
  • A. Maniyeri Suresh
  • M. J. Sugalska
  • G. Klein-Raina
  • S. Raina

  - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES - Year 2022

  Lipopolysaccharide (LPS) constitutes the major component of the outer membrane and is essential for bacteria, such as Escherichia coli. Recent work has revealed the essential roles of LapB and LapC proteins in regulating LPS amounts; although, if any additional partners are involved is unknown. Examination of proteins co-purifying with LapB identified LapD as a new partner. The purification of LapD reveals that it forms a complex...

  Full text available to download