Megha Patro

ORCID: 0009-0004-2399-3831
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Research Areas
  • Protist diversity and phylogeny
  • Bacterial Genetics and Biotechnology
  • Genomics and Phylogenetic Studies
  • Protein Structure and Dynamics
  • Photosynthetic Processes and Mechanisms
  • Yersinia bacterium, plague, ectoparasites research
  • Microbial Community Ecology and Physiology
  • Bacteriophages and microbial interactions
  • Methane Hydrates and Related Phenomena
  • RNA and protein synthesis mechanisms
  • Advanced biosensing and bioanalysis techniques
  • Algal biology and biofuel production
  • Enzyme Structure and Function

University of Freiburg
2020-2024

University of Groningen
2019

MinD proteins are well studied in rod-shaped bacteria such as E. coli, where they display self-organized pole-to-pole oscillations that important for correct positioning of the Z-ring at mid-cell cell division. Archaea also encode belonging to family, but their functions unknown. homologous were found be widespread Euryarchaeota and form a sister group bacterial distinct from ParA other related ATPase families. We aimed identify function four archaeal model archaeon Haloferax volcanii....

10.1016/j.cub.2020.09.073 article EN cc-by-nc-nd Current Biology 2020-10-30

Protein translocation across the bacterial cytoplasmic membrane is an essential process catalyzed by Sec translocase, which in its minimal form consists of protein-conducting channel SecYEG, and motor ATPase SecA. SecA binds via positively charged N-terminus to membranes containing anionic phospholipids, leading a lipid-bound intermediate. This interaction induces conformational change SecA, resulting high-affinity association with initiates protein translocation. Here, we examined effect...

10.1016/j.bbamem.2019.183035 article EN cc-by Biochimica et Biophysica Acta (BBA) - Biomembranes 2019-08-05

In bacteria and archaea, proteins of the ParA/MinD family ATPases regulate spatiotemporal organization various cellular cargoes, including cell division proteins, motility structures, chemotaxis systems, chromosomes. bacteria, such as

10.1101/2024.08.01.606218 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2024-08-01

Haloferax volcanii and other Haloarchaea can be pleomorphic, adopting different shapes, which vary with growth stages. Several studies have shown that H. cell shape is sensitive to various external factors including media physical environment. In addition, several noticed the presence of a recombinant plasmid in cells also factor impacting shape, notably by favoring development rods early stages growth. Here we investigated reasons for this phenomenon first studying impact auxotrophic...

10.3389/fmicb.2023.1270665 article EN cc-by Frontiers in Microbiology 2023-09-29

MinD proteins are well studied in rod-shaped bacteria such as E. coli , where they display self-organized pole-to-pole oscillations that important for correct positioning of the Z-ring at mid-cell cell division. Archaea also encode belonging to family, but their functions unknown. homologous were found be widespread Euryarchaeota and form a sister group bacterial distinct from ParA other related ATPase families. We aimed identify function four archaeal model archaeon Haloferax volcanii ....

10.1101/2020.04.03.021790 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2020-04-04

In bacteria and archaea, proteins of the ParA/MinD family ATPases regulate spatiotemporal organization various cellular cargoes, including cell division proteins, motility structures, chemotaxis systems, chromosomes. bacteria, such as

10.3389/fmicb.2024.1474570 article EN cc-by Frontiers in Microbiology 2024-11-12

Abstract Signal transduction via phosphorylated CheY towards the flagellum and archaellum involves a conserved mechanism of phosphorylation subsequent conformational changes within CheY. This is among bacteria archaea, despite substantial differences in composition architecture flagellum, respectively. Phosphorylated has higher affinity bacterial C-ring its binding leads to flagellar motor rotational switching flagellum. In adaptor protein CheF resides at cytoplasmic face archaeal formed by...

10.1038/s41467-022-30358-9 article EN cc-by Nature Communications 2022-05-23
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