Its sequence bears weak homology to a prokaryotic factor SulA that is involved in the inhibition of FtsZ polymerization in prokaryotic cells (Raynaud et al., 2004) so it could conceivably be involved in FtsZ polymerization dynamics inside the chloroplast.
Difference imaging; subtracting frame n- from frame n- might also be beneficial in analyzing where in the cell polymerization dynamics occur.
A consequence of reduced heterodimers might be a reduction of incorporated S140G tubulin into microtubules, which may in turn affect polymerization dynamics.
However, prior studies of this mutant have not directly examined its polymerization dynamics in vivo or in vitro (Machin et al., 1995; Dorn et al., 2005).
To obtain insight into how the mutation affects polymerization dynamics in cells, we used time lapse imaging in GFP-Tub1p expressing strains to measure microtubule dynamics of wild-type and β T238A-containing yeast.
The molecular mechanism by which the β T238A mutation affects microtubule dynamics is unknown, in part because the polymerization dynamics of β T238A αβ-tubulin have not been studied in vivo or in vitro.
As dynacortin localizes to actin-rich dynamic cortical domains, we determined whether dynacortin contributes to the bulk actin polymerization dynamics in the cell.
To monitor the spatiotemporal pattern of actin polymerization dynamics in response to budded yeast, we combined an mRFP-LimEΔ label for filamentous actin with a GFP-coronin label.
In the case of actin, polymerization dynamics are drastically affected by end-capping proteins, polymerization enhancers (e.g. formins) or filament stabilizers (e.g. tropomyosins), depolymerization enhancers (e.g. cofilin), and induced filament severing, (as depicted in Figure 3).
Changes in the nature of this job matching process can lead to changes in employment dynamics.
