The dmf1/mid1 gene is essential for correct positioning of the division septum in fission yeast.

Details

Serval ID
serval:BIB_C567BC2AE9C4
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The dmf1/mid1 gene is essential for correct positioning of the division septum in fission yeast.
Journal
Genes and Development
Author(s)
Sohrmann M., Fankhauser C., Brodbeck C., Simanis V.
Publication state
Published
Issued date
11/1996
Volume
10
Number
21
Pages
2707-2719
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
Little is known about the mechanisms that establish the position of the division plane in eukaryotic cells. Wild-type fission yeast cells divide by forming a septum in the middle of the cell at the end of mitosis. Dmf1 mutants complete mitosis and initiate septum formation, but the septa that form are positioned at random locations and angles in the cell, rather than in the middle. We have cloned the dmf1 gene as a suppressor of the cdc7-24 mutant. The dmf1 mutant is allelic with mid1. The gene encodes a novel protein containing a putative nuclear localization signal, and a carboxy-terminal PH domain. In wild-type cells, Dmf1p is nuclear during interphase, and relocates to form a medial ring at the cell cortex coincident with the onset of mitosis. This relocalization occurs before formation of the actin ring and is associated with increased phosphorylation of Dmf1p. The Dmf1p ring can be formed in the absence of an actin ring, but depends on some of the genes required for actin ring formation. When the septum is completed and the cells separate, Dmf1p staining is once again nuclear. These data implicate Dmf1p as an important element in assuring correct placement of the division septum in Schizosaccharomyces pombe cells.
Keywords
Amino Acid Sequence, Cell Division/genetics, Cloning, Molecular, Fungal Proteins/genetics, Membrane Glycoproteins/genetics, Molecular Sequence Data, Mutation, Phosphorylation, Protein Kinases/metabolism, Saccharomyces cerevisiae Proteins, Schizosaccharomyces/cytology, Schizosaccharomyces/enzymology
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 15:29
Last modification date
28/06/2023 5:55
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