Document Detail

The Sda1 protein is required for passage through start.
MedLine Citation:
PMID:  11160833     Owner:  NLM     Status:  MEDLINE    
We have used affinity chromatography to identify proteins that interact with Nap1, a protein previously shown to play a role in mitosis. Our studies demonstrate that a highly conserved protein called Sda1 binds to Nap1 both in vitro and in vivo. Loss of Sda1 function causes cells to arrest uniformly as unbudded cells that do not increase significantly in size. Cells arrested by loss of Sda1 function have a 1N DNA content, fail to produce the G1 cyclin Cln2, and remain responsive to mating pheromone, indicating that they arrest in G1 before Start. Expression of CLN2 from a heterologous promoter in temperature-sensitive sda1 cells induces bud emergence and polarization of the actin cytoskeleton, but does not induce cell division, indicating that the sda1 cell cycle arrest phenotype is not due simply to a failure to produce the G1 cyclins. The Sda1 protein is absent from cells arrested in G0 and is expressed before Start when cells reenter the cell cycle, further suggesting that Sda1 functions before Start. Taken together, these findings reveal that Sda1 plays a critical role in G1 events. In addition, these findings suggest that Nap1 is likely to function during G1. Consistent with this, we have found that Nap1 is required for viability in cells lacking the redundant G1 cyclins Cln1 and Cln2. In contrast to a previous study, we have found no evidence that Sda1 is required for the assembly or function of the actin cytoskeleton. Further characterization of Sda1 is likely to provide important clues to the poorly understood mechanisms that control passage through G1.
Z A Zimmerman; D R Kellogg
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular biology of the cell     Volume:  12     ISSN:  1059-1524     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2001 Jan 
Date Detail:
Created Date:  2001-02-22     Completed Date:  2001-09-06     Revised Date:  2013-04-17    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  201-19     Citation Subset:  IM    
Sinsheimer Labs, Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Cruz, Santa Cruz, California 95064, USA.
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MeSH Terms
Cell Cycle / drug effects*
Cell Cycle Proteins / genetics,  metabolism,  pharmacology*
Chromatography, Affinity
Cyclin G
Cyclins / drug effects,  metabolism
G1 Phase / drug effects
Nuclear Proteins*
Nucleosome Assembly Protein 1
Protein Binding
Proteins / metabolism
RNA, Ribosomal / drug effects
Saccharomyces cerevisiae Proteins*
Two-Hybrid System Techniques
Yeasts / genetics,  physiology
Reg. No./Substance:
0/Cell Cycle Proteins; 0/Cyclin G; 0/Cyclins; 0/NAP1 protein, S cerevisiae; 0/Nuclear Proteins; 0/Nucleosome Assembly Protein 1; 0/Proteins; 0/RNA, Ribosomal; 0/SDA1 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins

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