Premium
A Bnr‐like formin links actin to the spindle pole body during sporulation in the filamentous fungus Ashbya gossypii
Author(s) -
Kemper Michael,
Mohlzahn Lars,
Lickfeld Manuela,
Lang Claudia,
Wählisch Sabrina,
Schmitz HansPeter
Publication year - 2011
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2011.07644.x
Subject(s) - biology , formins , sporangium , microbiology and biotechnology , centrosome , actin , spore , spindle pole body , filamentous fungus , actin cytoskeleton , cytoskeleton , botany , spindle apparatus , genetics , gene , cell division , cell , cell cycle
Summary Formin proteins are nucleators of actin filaments and regulators of the microtubule cytoskeleton. As such, they play important roles in the development of yeast and other fungi. We show here that Ag Bnr2, a homologue of the Sc Bnr1 formin from the filamentous fungus Ashbya gossypii , localizes to the spindle pole body (SPB), the fungal analogue of the centrosome of metazoans. This protein plays an important role in the development of the typical needle‐shaped spores of A. gossypii , as suggested by several findings. First, downregulation of AgBNR2 causes defects in sporangium formation and a decrease in the total spore number. Second, a fusion of AgBNR2 to GFP that is driven by the native AgBNR2 promoter is only visible in sporangia. Third, Ag Bnr2 interacts with a Ag Spo21, a sporulation‐specific component of the SPB. Furthermore, we provide evidence that Ag Bnr2 might nucleate actin cables, which are connected to SPBs during sporulation. Our findings add to our understanding of fungal sporulation, particularly the formation of spores with a complex, elongated morphology, and provide novel insights into formin function.