Open AccessThe involvement of the Schizosaccharomyces pombe sep9/spt8 + gene in the regulation of septum cleavage
Author(s) -
Batta Gyula,
Szilagyi Zsolt,
Laczik Miklos,
Sipiczki Matthias
Publication year - 2009
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2009.00522.x
Subject(s) - schizosaccharomyces pombe , biology , schizosaccharomyces , cleavage (geology) , gene , genetics , microbiology and biotechnology , saccharomyces cerevisiae , paleontology , fracture (geology)
Schizosaccharomyces cells divide by medial septation, followed by enzymatic degradation of parts of the septum (septum cleavage) to allow the sister cells to separate from each other. In a previous study we found that the cell separation mutant sep9‐307 was defective in a gene that encodes a protein highly similar in sequence to the Saccharomyces cerevisiae protein Spt8, a subunit of the SAGA complex. Here, we show that the sep9‐307 mutation causes a frameshift in translation. The deletion of sep9 + is not lethal but abolishes normal septum cleavage by reducing the activity of ace2 + , a gene coding for a transcription factor of numerous genes producing proteins for septum cleavage. Indirect evidence indicates that Sep9 might also act directly in the transcription of certain target genes (e.g. eng1 + ) of this regulator. sep9‐307 is synthetically lethal with mutations in the cell separation genes sep11/med18 + and sep15/med8 + , which encode subunits of the general transcription factor mediator. Heterologous expression of SPT8 and the putative Schizosaccharomyces japonicus sep9 + orthologue cannot substitute for sep9 + . Both Spt8 and the fission yeast proteins have highly acidic (74–76 amino‐acid long) N‐terminal regions with no sequence conservation.