Ks. Bruno et al., SEPH, a Cdc7p orthologue from Aspergillus nidulans, functions upstream of actin ring formation during cytokinesis, MOL MICROB, 42(1), 2001, pp. 3-12
In the filamentous fungus, Aspergillus nidulans, multiple rounds of nuclear
division occur before cytokinesis, allowing an unambiguous identification
of genes required specifically for cytokinesis. As in animal cells, both an
intact microtubule cytoskeleton and progression through mitosis are requir
ed for actin ring formation and contraction. The sepH gene from A. nidulans
was discovered in a screen for temperature-sensitive cytokinesis mutants.
Sequence analysis showed that SEPH is 42% identical to the serine-threonine
kinase Cdc7p from fission yeast. Signalling through the (S) under bar epta
tion (I) under bar nitiation (N) under bar etwork (SIN), which includes Cdc
7p and the GTPase Spg1p, is emerging as a primary regulatory pathway used b
y fission yeast to control cytokinesis. A similar group of proteins compris
e the Mitotic Exit Network (MEN) in budding yeast. This is the first direct
evidence for the existence of a functional SIN-MEN pathway outside budding
and fission yeast. In addition to SEPH, potential homologues were also ide
ntified in other fungi and plants but not in animal cells. Deletion of sepH
resulted in a viable strain that failed to septate at any temperature. Int
erestingly, quantitative analysis of the actin cytoskeleton revealed that s
epH is required for construction of the actin ring. Therefore, SEPH is dist
inct from its counterpart in fission yeast, in which SIN components operate
downstream of actin ring formation and are necessary for ring contraction
and later events of septation. We conclude that A. nidulans has components
of a SIN-MEN pathway, one of which, SEPH, is required for early events duri
ng cytokinesis.