(C ) Each chromosome arm is translocated by a different SpoIIIE channel that is comprised of opposing motor domains that have the ability to export DNA from their respective cell.
Consequently, the mother cell-SpoIIIE exports DNA until the final loop (ter ) reaches the septum.
We show that SpoIIIE can operate, in principle, as a bi-directional motor that exports DNA.
In the absence of the mother cell protein, forespore SpoIIIE translocates the chromosome out of the forespore, indicating that SpoIIIE exports DNA.
Moreover, we show that SpoIIIE can operate, in principle, as a bi-directional motor that exports DNA from a given cell compartment.
Prior to the establishment of directional DNA translocation, both complexes could, in principle, export DNA out of its respective compartment (Sharp and Pogliano, 2002; Becker and Pogliano, 2007; Ptacin et al., 2008), leading to a potential clash between complexes in each cell; as a result, these complexes would compete to translocate DNA either out of or into the forespore.
It is well documented that glyceraldehyde 3-phosphate dehydrogenase mRNA levels are not always constant [ 63, 67, 70], and it contributes to diverse cellular functions, such as nuclear RNA export, DNA replication, DNA repair, exocytotic membrane fusion, cytoskeletal organisation and phosphotransferase activity [ 71].
They further showed that the SpoIIIE complex functions to export the DNA out of the cell, and only the SpoIIIE complex on the mother cell side is required for the translocation of the DNA into the forespore.
The virB T4SS, which is known to export T-DNA from the bacterial cell into the plant cell is only found on the Ti-plasmid of A. tumefaciens.
We examined the relative contribution of import, export and DNA binding to the subcellular localization of NFAT5 in isotonic conditions.
