The Ccr4-Pop2-NOT mRNA deadenylase contributes to septin organization in Saccharomyces cerevisiae

Date

2009

Authors

Traven, Ana
Beilharz, Traude H
Lo, Tricia L
Lueder, Franziska
Preiss, Thomas
Heierhorst, Jorg

Journal Title

Journal ISSN

Volume Title

Publisher

Genetics Society of America

Abstract

In yeast, assembly of the septins at the cell cortex is required for a series of key cell cycle events: bud-site selection, the morphogenesis and mitotic exit checkpoints, and cytokinesis. Here we establish that the Ccr4-Pop2-NOT mRNA deadenylase contributes to septin organization. mRNAs encoding regulators of septin assembly (Ccd42, Cdc24, Rga1, Rga2, Bem3, Gin4, Cla4, and Elm1) presented with short poly(A) tails at steady state in wild-type (wt) cells, suggesting their translation could be restricted by deadenylation. Deadenylation of septin regulators was dependent on the major cellular mRNA deadenylase Ccr4-Pop2-NOT, whereas the alternative deadenylase Pan2 played a minor role. Consistent with deadenylation of septin regulators being important for function, deletion of deadenylase subunits CCR4 or POP2, but not PAN2, resulted in septin morphology defects (e.g., ectopic bud-localized septin rings), particularly upon activation of the Cdc28-inhibitory kinase Swe1. Aberrant septin staining was also observed in the deadenylase-dead ccr4-1 mutant, demonstrating the deadenylase activity of Ccr4-Pop2 is required. Moreover, ccr4Δ, pop2Δ, and ccr4-1 mutants showed aberrant cell morphology previously observed in septin assembly mutants and exhibited genetic interactions with mutations that compromise septin assembly (shs1Δ, cla4Δ, elm1Δ, and gin4Δ). Mutations in the Not subunits of Ccr4-Pop2-NOT, which are thought to predominantly function in transcriptional control, also resulted in septin organization defects. Therefore, both mRNA deadenylase and transcriptional functions of Ccr4-Pop2-NOT contribute to septin organization in yeast.

Description

Keywords

Keywords: Bem3 protein; ccr4 pop2 not mrna deadenylase; Cla4 protein; cyclin dependent kinase 1; Elm1 protein; Gin4 protein; guanosine triphosphatase activating protein; mutant protein; phosphotransferase; polynucleotide adenylyltransferase; protein Cdc42; Rga1 pro

Citation

Source

Genetics (online)

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1534/genetics.109.104414

Restricted until

2037-12-31