XXXX dynamin-like 2 that binds specifically to @entity1076 assembles into a high-molecular weight complex in vivo and in vitro.

@entity958 @entity1219 @entity2164 @entity3006 @entity59234 @entity1076 @entity526
@entity59234 , a member of the high-molecular weight (M(r)) dynamin family found in @entity958 , has been shown to be targeted to the plastid. In the chloroplast, most of the @entity59234 was present in the fraction containing the envelope membranes when analyzed by suborganellar fractionation. Sucrose gradient and gel filtration experiments showed that when associated with membranes, @entity59234 existed as a high-M(r) complex, whereas the soluble form existed as a monomer. The recombinant @entity59234 expressed in @entity526 was present as a high-M(r) form and showed higher GTPase activity at a low @entity1219 concentration, whereas @entity59234 existed as a low-M(r) form with a low level of GTPase activity at a high @entity1219 concentration. Electron microscopy studies revealed that the purified recombinant @entity59234 formed spiral-coiled structures or rings. In the presence of @entity2164 , these structures were transformed into a long rod structure. In contrast, in the presence of @entity3006 , these structures disassembled into oligomers that were shown to be tetramer with 4-fold symmetry. Finally, a lipid-binding assay revealed that recombinant @entity59234 purified from @entity526 bound specifically to @entity1076 . Together, these results demonstrated that the biochemical properties of @entity59234 were very similar to those of dynamin and other related proteins. Based on this similarity, we propose that @entity59234 may be involved in vesicle formation at the chloroplast envelope membrane.
