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PMID: 9096347 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Target of rapamycin proteins and their kinase activities are required for meiosis.

Zheng XF, Schreiber SL

Abstract

The phosphatidylinositol kinase-related kinases, including Tor1p, Tor2p, FRAP/RAFT, FRP/ATR, ATM, Mec1p, Rad3, and Tel1p, function in signal transduction pathways involved in cell cycle progression and surveillance. The rapamycin-sensitive kinase activities of Tor1p and Tor2p are required for the nutrient-activated protein translation essential for G1 cell cycle progression in haploid yeast cells. In addition, Tor2p's kinase activity is necessary for its unique rapamycin-insensitive function involved in the assembly of the actin cytoskeleton. In the current study using diploid yeast, we found that the kinase activities of the Tor proteins are also required for two discrete steps during yeast meiosisthe switch between the mitotic and meiotic cell cycles and a later step during meiosis involved in the packaging of resultant haploid cells (spores) into asci. Based on what is known of the mitotic functions of Tor and FRAP proteins, these results likely reflect the requirement for signaling pathways leading to regulated protein translation during meiosis. Mec1p, which is required for meiotic recombination, and the Tor proteins are, therefore, homologous kinases with distinct, yet essential, roles in meiosis.

MeSH Terms
1-Phosphatidylinositol 4-Kinase Culture Media Fungal Proteins/metabolism,physiology Meiosis/physiology Phosphotransferases (Alcohol Group Acceptor)/metabolism Polyenes/metabolism Saccharomyces cerevisiae/cytology,metabolism Saccharomyces cerevisiae Proteins Sirolimus
Chemicals
Culture Media Fungal Proteins Polyenes Saccharomyces cerevisiae Proteins Phosphotransferases (Alcohol Group Acceptor) 1-Phosphatidylinositol 4-Kinase PIK1 protein, S cerevisiae Sirolimus
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Zheng X F
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Schreiber S L
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17 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1997-04-01
Pages
3070-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC20323
Subset
IM
Grants
NIGMS NIH HHS · R01 GM038627 · United States
NIGMS NIH HHS · R37 GM038627 · United States
NIGMS NIH HHS · GM38627 · United States
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