Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-6-16
pubmed:abstractText
The nudA1 mutation in the cytoplasmic dynein heavy chain gene inhibits nuclear migration, colony growth and asexual sporulation (conidiation) in the filamentous fungus Aspergillus nidulans. It also alters the location of the first cell division event (septation) and prevents nucleation of tip cells. We showed previously that a suppressor of nudA1, snaD290, partially reversed the nuclear migration defect and partially restored colony growth. We have now demonstrated that the snaD290 mutation also delays septation and restores the septum to its normal position, allowing tip cells to be nucleated. Although snaD290 does not affect nuclear migration or vegetative hyphal growth, it almost completely inhibits conidiation. We propose that the SNAD protein participates in septation, and is essential for asexual spore formation. SnaD encodes a novel 76-kDa coiled-coil protein (SNAD) that is located at the spindle pole body throughout the cell cycle. Therefore, our results suggest that proteins at the spindle pole body are likely to be involved in temporal regulation of septation in A. nidulans.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0026-8925
pubmed:author
pubmed:issnType
Print
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
375-87
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10821171-Actins, pubmed-meshheading:10821171-Amino Acid Sequence, pubmed-meshheading:10821171-Aspergillus nidulans, pubmed-meshheading:10821171-Blotting, Western, pubmed-meshheading:10821171-Cell Cycle Proteins, pubmed-meshheading:10821171-Cell Division, pubmed-meshheading:10821171-Cell Nucleus, pubmed-meshheading:10821171-Cloning, Molecular, pubmed-meshheading:10821171-Fungal Proteins, pubmed-meshheading:10821171-Genetic Complementation Test, pubmed-meshheading:10821171-Green Fluorescent Proteins, pubmed-meshheading:10821171-Luminescent Proteins, pubmed-meshheading:10821171-Microtubules, pubmed-meshheading:10821171-Models, Genetic, pubmed-meshheading:10821171-Molecular Sequence Data, pubmed-meshheading:10821171-Mutagenesis, pubmed-meshheading:10821171-Phenotype, pubmed-meshheading:10821171-Sequence Analysis, DNA, pubmed-meshheading:10821171-Suppression, Genetic, pubmed-meshheading:10821171-Tubulin
pubmed:year
2000
pubmed:articleTitle
A spindle pole body-associated protein, SNAD, affects septation and conidiation in Aspergillus nidulans.
pubmed:affiliation
Department of Pharmacology, UMDNJ/RWJMS, Piscataway, NJ 08854, USA. bliu@ucdavis.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.