Abstract:
:The ro mutants of Neurospora crassa are defective in nuclear migration and hyphal morphogenesis. Several of the ro loci have recently been shown to encode components of the dynein/dynactin motor complex. Here we report on the cloning and characterization of the ro-2 gene which codes for a novel 80 kDa protein that has two Cys-rich motifs which resemble zinc-binding LIM or RING domains thought to mediate protein-protein interactions. RO2 also contains several potential binding sites for Src homology 3 (SH3) domains. The ro-2B20 allele has a frameshift mutation within one of the Cys-rich domains which eliminates the C-terminal half of the open reading frame (ORF). Disruption of the ro-2 locus by repeat-induced point (RIP) mutation gave rise to progeny which have a nuclear migration defect, but which are also blocked in conidiation. The ability to assemble cytoplasmic microtubules and actin is maintained in ro-2 mutants, although subapical actin patches are more prominent. Based on these observations, the RO2 gene product is proposed to play a role in mediating interactions between components of the dynein/dynactin motor complex or in linking this complex to the nucleus or cytoskeleton.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Vierula PJ,Mais JMdoi
10.1046/j.1365-2958.1997.3461704.xsubject
Has Abstractpub_date
1997-04-01 00:00:00pages
331-40issue
2eissn
0950-382Xissn
1365-2958journal_volume
24pub_type
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