MinD2 modulates cell shape and motility in the archaeon .

In bacteria and archaea, proteins of the ParA/MinD family of ATPases regulate the spatiotemporal organization of various cellular cargoes, including cell division proteins, motility structures, chemotaxis systems, and chromosomes. In bacteria, such as , MinD proteins are crucial for the correct placement of the Z-ring at mid-cell during cell division. However, previous studies have shown that none of the 4 MinD homologs present in the archaeon have a role in cell division, suggesting that these proteins regulate different cellular processes in haloarchaea.

MinD2 modulates cell shape and motility in the archaeon .

In bacteria and archaea, proteins of the ParA/MinD family of ATPases regulate the spatiotemporal organization of various cellular cargoes, including cell division proteins, motility structures, chemotaxis systems, and chromosomes. In bacteria, such as , MinD proteins are crucial for the correct placement of the Z-ring at mid-cell during cell division. However, previous studies have shown that none of the 4 MinD homologs present in the archaeon have a role in cell division, suggesting that these proteins regulate different cellular processes in haloarchaea.

"Influence of plasmids, selection markers and auxotrophic mutations on cell shape plasticity".

and other Haloarchaea can be pleomorphic, adopting different shapes, which vary with growth stages. Several studies have shown that cell shape is sensitive to various external factors including growth media and physical environment. In addition, several studies have noticed that the presence of a recombinant plasmid in the cells is also a factor impacting cell shape, notably by favoring the development of rods in early stages of growth.

Methods to Analyze Motility in Eury- and Crenarchaea.

Many archaea display swimming motility in liquid medium, which is empowered by the archaellum. Directional movement requires a functional archaellum and a sensing system, such as the chemotaxis system that is used by Euryarchaea. Two well-studied models are the euryarchaeon Haloferax volcanii and the crenarchaeon Sulfolobus acidocaldarius.

Structural insights into the mechanism of archaellar rotational switching.

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

An Oscillating MinD Protein Determines the Cellular Positioning of the Motility Machinery in Archaea.

MinD proteins are well studied in rod-shaped bacteria such as E. coli, where they display self-organized pole-to-pole oscillations that are important for correct positioning of the Z-ring at mid-cell for cell division. Archaea also encode proteins belonging to the MinD family, but their functions are unknown.

Two distinct anionic phospholipid-dependent events involved in SecA-mediated protein translocation.

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