Question

A researcher extracts the cytosol and cytoskeletal components from the cell and places the mixture into a tube. What result do you expect if the researcher adds a nonhydrolyzable GTP analog to the mixture in vitro?

Answer 1

Adding a nonhydrolyzable GTP analog would disrupt the normal function of microtubules and motor proteins by preventing their assembly and disassembly processes, potentially leading to the stabilization of microtubules and interrupting cell division.

Step-by-step explanation:

If a researcher adds a nonhydrolyzable GTP analog to a mixture of cytosol and cytoskeletal components in vitro, it is likely that the cytoskeletal structures, particularly microtubules and motor proteins that would normally use GTP for assembly and disassembly processes, would not be able to properly function. GTP is required for the polymerization and depolymerization of tubulin subunits that make up microtubules, as mentioned in the reference provided. Therefore, with a nonhydrolyzable GTP analog, these normal dynamics would be disrupted, potentially leading to stabilization of microtubules without permitting their usual dynamic instability. Similarly, motor proteins like dynamin, which require GTP hydrolysis for the scission of vesicles during endocytosis, would likely be unable to proceed with vesicle formation and release. This could also impact cell division, as components like FtsZ and tubulin which require GTP would not be able to undergo their normal cycles of rapid assembly and disassembly, crucial for the cell division process.