Not only must the complex locate subordinate subcomplexes, but it must itself be
a subcomplex of another, perhaps more pervasive, complex.
Not exact matches
The project focuses on the dynamics
of transient microcompartments formed by the V - ATPase holoenzyme, V - ATPase
subcomplexes and subunits together with the mentioned proteins, with the aim to understand the mechanisms leading to this unique type
of physiologically relevant regulation.
For this purpose analyze, on the one hand, the interaction
of the V - ATPase, its
subcomplexes and subunits with the mentioned proteins biochemically and by cryo - electron microscopy.
Determination
of the structure
of the entire complex was possible only through this step - by - step approach, building on from smaller
subcomplexes towards the entire assembly.
We show here that the S. cerevisiae Csm1 / Lrs4 monopolin
subcomplex has a distinctive V - shaped structure, with two pairs
of protein - protein interaction domains positioned approximately 10 nm apart.