A potential functional relationship between phosphorylation by mitotic kinases and protein methylation by the Set1 complex in Aspergillus nidulans.

Ref ID: 18363

Author:

Meera Govindaraghavan , Sarah Lea McGuire and Stephen A. Osmani

Author address:

Department of Molecular Genetics, The Ohio State University,
1 2 1 1
Columbus, OH, Department of Biology, Millsaps College, Jackson, MS, govindaraghvan.1@buckeyemail.osu.edu,
osmani.2@osu.edu

Full conference title:

Asperfest 8

Abstract:

The G2-M transition is regulated by the activity of two mitotic kinases, NIMA and NIMX, in Aspergillus nidulans. To gain further insight into the
mechanism of NIMA function, a synthetic lethal screen was carried out utilizing the deletion of the non-essential nimA orthologue, KIN3, in
Saccharomyces cerevisiae. This screen revealed a set of 11 genes involved in different cellular processes. By deletion analysis, four of these synthetic
genetic interactions were found to be conserved in A. nidulans, one of which is between nimA7 and the deletion of An- swd1, the ortholog of a subunit
ts
of the Set1 methyl transferase complex. Moreover, the synthetic lethal interaction between ?An-swd1 and a cell cycle mutant with reduced NIMX function
(nimT23 ) suggests that lack of An-swd1 function in combination with defectsin G2-M transition is highly deleterious. These genetic interactions result
ts
from loss of protein methyl transferase activity of the Set1 complex, since the deletion of An- set1, which encodes the catalytic protein, also exhibits
genetic interaction with nimA7 and nimT23 . Interestingly, the deletion of An-swd1 also modifies the nimA7 and nimT23 phenotypes at their fully
ts ts
restrictive temperature, causing a drastic growth defect. Furthermore, a proportion of nimA7+?An-swd1 cells are uninucleated yet undergo septation, a
phenotype never observed in either single mutant. Collectively these results indicate an important functional relationship exists between mitotic protein
phosphorylation and protein methylation.
govind.meera@gmail.com

Abstract Number: 41)

Conference Year: 2011

Link to conference website: NULL

New link: NULL

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