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Vol. 13, Issue 8, 2747-2759, August 2002
*Laboratory of Biochemistry and Genetics, National Institute of
Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892;
and Actomyosin ring contraction and chitin primary septum deposition
are interdependent processes in cell division of budding yeast. By
fusing Myo1p, as representative of the contractile ring, and Chs2p for
the primary septum, to different fluorescent proteins we show herein
that the two processes proceed essentially at the same location and
simultaneously. Chs2p differs from Myo1p in that it reflects the
changes in shape of the plasma membrane to which it is attached and in
that it is packed after its action into visible endocytic vesicles for
its disposal. To ascertain whether this highly coordinated system could
function independently of other cell cycle events, we reexamined the
septum-like structures made by the septin mutant cdc3 at
various sites on the cell cortex at the nonpermissive temperature. With
the fluorescent fusion proteins mentioned above, we observed that in
cdc3 at 37°C both Myo1p and Chs2p colocalize at
different spots of the cell cortex. A contraction of the Myo1p patch
could also be detected, as well as that of a Chs2p patch, with
subsequent appearance of vesicles. Furthermore, the septin Cdc12p,
fused with yellow or cyan fluorescent protein, also colocalized with
Myo1p and Chs2p at the aberrant locations. The formation of delocalized
septa did not require nuclear division. We conclude that the septation
apparatus, composed of septins, contractile ring, and the chitin
synthase II system, can function at ectopic locations autonomously and
independently of cell division, and that it can recruit the other
elements necessary for the formation of secondary septa.
Laboratory of Cell Biology, National Heart, Lung, and
Blood Institute, Bethesda, Maryland 20892
Corresponding author. E-mail address:
enricoc{at}bdg10.niddk.nih.gov.
Online version of this article
contains video material for some figures. Online version available at
www.molbiolcell.org.
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