The Aspergillus nidulans IQGAP orthologue SepG is required for constriction of the contractile actomyosin ring.

Autor: Hill TW; Department of Biology, Rhodes College, Memphis, TN 38112, USA; Biochemistry and Molecular Biology Program, Rhodes College, Memphis, TN 38112, USA. Electronic address: hill@rhodes.edu., Wendt KE; Biochemistry and Molecular Biology Program, Rhodes College, Memphis, TN 38112, USA., Jones DA; Department of Chemistry, Rhodes College, Memphis, TN 38112, USA., Williamson MH; Biochemistry and Molecular Biology Program, Rhodes College, Memphis, TN 38112, USA., Ugwu UJ; Division of Natural & Mathematic Sciences, LeMoyne-Owen College, Memphis, TN 38126, USA., Rowland LB; Biochemistry and Molecular Biology Program, Rhodes College, Memphis, TN 38112, USA., Jackson-Hayes L; Biochemistry and Molecular Biology Program, Rhodes College, Memphis, TN 38112, USA; Department of Chemistry, Rhodes College, Memphis, TN 38112, USA.
Jazyk: angličtina
Zdroj: Fungal genetics and biology : FG & B [Fungal Genet Biol] 2020 Nov; Vol. 144, pp. 103439. Date of Electronic Publication: 2020 Aug 06.
DOI: 10.1016/j.fgb.2020.103439
Abstrakt: In this research we report that the sepG1 mutation in Aspergillus nidulans resides in gene AN9463, which is predicted to encode an IQGAP orthologue. The genetic lesion is predicted to result in a G-to-R substitution at residue 1637 of the 1737-residue protein in a highly conserved region of the RasGAP-C-terminal (RGCT) domain. When grown at restrictive temperature, strains expressing the sepG G1637R (sepG1) allele are aseptate, with reduced colony growth and aberrantly formed conidiophores. The aseptate condition can be replicated by deletion of AN9463 or by downregulating its expression via introduced promoters. The mutation does not prevent assembly of a cortical contractile actomyosin ring (CAR) at putative septation sites, but tight compaction of the rings is impaired and the rings fail to constrict. Both GFP::SepG wild type and the GFP-tagged product of the sepG1 allele localize to the CAR at both permissive and restrictive temperatures. Downregulation of myoB (encoding the A. nidulans type-II myosin heavy chain) does not prevent formation of SepG rings at septation sites, but filamentous actin is required for CAR localization of SepG and MyoB. We identify fourteen probable IQ-motifs (EF-hand protein binding sites) in the predicted SepG sequence. Two of the A. nidulans EF-hand proteins, myosin essential light chain (AnCdc4) and myosin regulatory light chain (MrlC), colocalize with SepG and MyoB at all stages of CAR formation and constriction. However, calmodulin (CamA) appears at septation sites only after the CAR has become fully compacted. When expression of sepG is downregulated, leaving MyoB as the sole IQ-motif protein in the pre-compaction CAR, both MrlC and AnCdc4 continue to associate with the forming CAR. When myoB expression is downregulated, leaving SepG as the sole IQ-motif protein in the CAR, AnCdc4 association with the forming CAR continues but MrlC fails to associate. This supports a model in which the IQ motifs of MyoB bind both MrlC and AnCdc4, while the IQ motifs of SepG bind only AnCdc4. Downregulation of either mrlC or Ancdc4 results in an aseptate phenotype, but has no effect on association of either SepG or MyoB with the CAR.
(Copyright © 2020 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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