Publications by authors named "R W Pickersgill"
Article Synopsis
- * Encapsulation peptides, which help target enzymes to these microcompartments, are shown to bind to a specific groove formed by the shell proteins, aiding in shell assembly.
- * Understanding how these peptides bind provides insight into the microcompartments' structure and function, potentially leading to applications in bioengineering or disease prevention.
Article Synopsis
- The phytopathogenic bacterium Dickeya dadantii uses the type 2 secretion system (T2SS) to release enzymes and factors that degrade plant cell walls and contribute to its virulence.
- The GspB protein plays a crucial role in assembling the secretin protein GspD, necessary for forming outer membrane pores, and affects the secretion of pectinase, an enzyme involved in plant cell wall degradation.
- Structural analyses show that GspB interacts with GspD and anchors secretin channels to the inner membrane, while phylogenetic studies reveal variations of GspB in other bacteria, indicating a diverse role in secretion systems.
Microtubules segregate chromosomes by attaching to macromolecular kinetochores. Only microtubule-end attached kinetochores can be pulled apart; how these end-on attachments are selectively recognised and stabilised is not known. Using the kinetochore and microtubule-associated protein, Astrin, as a molecular probe, we show that end-on attachments are rapidly stabilised by spatially-restricted delivery of PP1 near the C-terminus of Ndc80, a core kinetochore-microtubule linker.
View Article and Find Full Text PDFBacterial microcompartments, BMCs, are proteinaceous organelles that encase a specific metabolic pathway within a semi-permeable protein shell. Short encapsulation peptides can direct cargo proteins to the lumen of the compartments. However, the fusion of such peptides to non-native proteins does not guarantee encapsulation and often causes aggregation.
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