Previous Article | Next Article ![]()
Molecular and Cellular Biology, September 2000, p. 6646-6658, Vol. 20, No. 18
Department of Biochemistry and Cell Biology,
Institute for Cell and Developmental Biology, State University of
New York at Stony Brook, Stony Brook, New York
11794-5215,1 and Department of Cytology
and Genetics, Institute of Botany, University of Vienna, A-1030
Vienna, Austria2
Received 31 January 2000/Returned for modification 28 March
2000/Accepted 12 June 2000
In yeast, HOP1 and RED1 are required during
meiosis for proper chromosome segregation and the consequent formation
of viable spores. Mutations in either HOP1 or
RED1 create unique as well as overlapping phenotypes,
indicating that the two proteins act alone as well as in concert with
each other. To understand which meiotic processes specifically require
Red1p-Hop1p hetero-oligomers, a novel genetic screen was used to
identify a single-point mutation of RED1,
red1-K348E, that separates Hop1p binding from Red1p
homo-oligomerization. The Red1-K348E protein is stable, phosphorylated
in a manner equivalent to Red1p, and undergoes efficient
homo-oligomerization; however, its ability to interact with Hop1p both
by two-hybrid and coimmunoprecipitation assays is greatly reduced.
Overexpression of HOP1 specifically suppresses
red1-K348E, supporting the idea that the only defect in the
protein is a reduced affinity for Hop1p. red1-K348E mutants exhibit reduced levels of crossing over and spore viability and fail to
undergo chromosome synapsis, thereby implicating a role for Red1p-Hop1p
hetero-oligomers in these processes. Furthermore, red1-K348E suppresses the sae2/com1 defects in
meiotic progression and sporulation, indicating a previously unknown
role for HOP1 in the meiotic recombination checkpoint.
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Meiotic Segregation, Synapsis, and Recombination
Checkpoint Functions Require Physical Interaction between the
Chromosomal Proteins Red1p and Hop1p
*
Corresponding author. Mailing address: Department of
Biochemistry and Cell Biology, SUNY Stony Brook, Stony Brook, NY
11794-5215. Phone: (631) 632-8581. Fax: (631) 632-8575. E-mail:
nhollin{at}notes.cc.sunysb.edu.
This article has been cited by other articles:
| J. Bacteriol. | J. Virol. | Eukaryot. Cell |
|---|
| Microbiol. Mol. Biol. Rev. | Clin. Vaccine Immunol. | All ASM Journals |
|---|