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*suggest hidden layer of biological regulation
*maybe a fold as fundamental as P-loop ATPases or Rossmann folds (well, this has to be seen!)
*be a treasure trove of uncharacterized proteins waiting to be studied.
We probably have only scratched the surface.
*suggest hidden layer of biological regulation
*maybe a fold as fundamental as P-loop ATPases or Rossmann folds (well, this has to be seen!)
*be a treasure trove of uncharacterized proteins waiting to be studied.
We probably have only scratched the surface.
ParB-CTPase is like the Swiss Army knife.
*Sometimes it helps form a DNA clamp.
*Sometimes as an enzyme module.
*Sometimes may be as a scaffold.
Evolution keeps re-purposing it for new cellular roles.
ParB-CTPase is like the Swiss Army knife.
*Sometimes it helps form a DNA clamp.
*Sometimes as an enzyme module.
*Sometimes may be as a scaffold.
Evolution keeps re-purposing it for new cellular roles.
*In Bacillus, Noc uses CTP to coordinate DNA segregation with cell division.
*In Shigella/E.coli/Pseudomonas, VirB/KorB/BisD regulates gene expression with a CTP switch.
*In archaea/eukaryotes, some are kinases or sulfiredoxins.
*In Bacillus, Noc uses CTP to coordinate DNA segregation with cell division.
*In Shigella/E.coli/Pseudomonas, VirB/KorB/BisD regulates gene expression with a CTP switch.
*In archaea/eukaryotes, some are kinases or sulfiredoxins.
*Likely an ancient NTP-binding module
*Also found in plasmids, phages, & chromosomes
*Fused to lineage-specific domains
*Not limited to CTP - can also bind ATP and even GTP!!! (we purified 28 diverse proteins to test NTP preference).
A very versatile fold!
*Likely an ancient NTP-binding module
*Also found in plasmids, phages, & chromosomes
*Fused to lineage-specific domains
*Not limited to CTP - can also bind ATP and even GTP!!! (we purified 28 diverse proteins to test NTP preference).
A very versatile fold!
We surveyed 80,000+ proteins across bacteria, archaea, phages, and eukaryotes.
Result: the ParB-CTPase fold is EVERYWHERE.
Not just in chromosome segregation, but fused to diverse domains, often on mobile genetic elements.
We surveyed 80,000+ proteins across bacteria, archaea, phages, and eukaryotes.
Result: the ParB-CTPase fold is EVERYWHERE.
Not just in chromosome segregation, but fused to diverse domains, often on mobile genetic elements.
ParB uses CTP to clamp around DNA, recruit ParA (an ATPase), and ensure chromosomes are properly inherited by daughter cells. CTP hydrolysis then recycles ParB. This represents a new regulatory principle!
ParB uses CTP to clamp around DNA, recruit ParA (an ATPase), and ensure chromosomes are properly inherited by daughter cells. CTP hydrolysis then recycles ParB. This represents a new regulatory principle!
One class of such switches bind nucleotide triphosphate (ATP, GTP, etc.), flip “on/off,” and regulate essential processes: growth, DNA replication, protein synthesis.
For decades, only GTPase/ATPase switches were known. Then came CTPases.
One class of such switches bind nucleotide triphosphate (ATP, GTP, etc.), flip “on/off,” and regulate essential processes: growth, DNA replication, protein synthesis.
For decades, only GTPase/ATPase switches were known. Then came CTPases.