a genome-wide screen for regulators of torc1 in response to amino acid starvation reveals a conserved npr23 complex监管机构的全基因组屏幕torc1针对氨基酸饥饿揭示了一个守恒npr23复杂.pdfVIP
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a genome-wide screen for regulators of torc1 in response to amino acid starvation reveals a conserved npr23 complex监管机构的全基因组屏幕torc1针对氨基酸饥饿揭示了一个守恒npr23复杂
A Genome-Wide Screen for Regulators of TORC1 in
Response to Amino Acid Starvation Reveals a Conserved
Npr2/3 Complex
Taavi K. Neklesa1,2¤*, Ronald W. Davis 1,2
1 Department of Biochemistry, Stanford University, Stanford, California, United States of America, 2 Stanford Genome Technology Center, Palo Alto, California, United
States of America
Abstract
TORC1 is a central regulator of cell growth in response to amino acid availability, yet little is known about how it is
regulated. Here, we performed a reverse genetic screen in yeast for genes necessary to inactivate TORC1. The screen
consisted of monitoring the expression of a TORC1 sensitive GFP-based transcriptional reporter in all yeast deletion strains
using flow cytometry. We find that in response to amino acid starvation, but not to carbon starvation or rapamycin
treatment, cells lacking NPR2 and NPR3 fail to fully (1) activate transcription factors Gln3/Gat1, (2) dephosphorylate TORC1
effector Npr1, and (3) repress ribosomal protein gene expression. Both mutants show proliferation defects only in media
containing a low quality nitrogen source, such as proline or ammonia, whereas no defects are evident when cells are grown
in the presence of glutamine or peptone mixture. Proliferation defects in npr2D and npr3D cells can be completely rescued
by artificially inhibiting TORC1 by rapamycin, demonstrating that overactive TORC1 in both strains prevents their ability to
adapt to an environment containing a low quality nitrogen source. A biochemical purification of each demonstrates that
Npr2 and Npr3 form a heterodimer, and this interaction is evolutionarily conserved since the human homologs of NPR2 and
NPR3 (NPRL2 and NPRL3, respectively) also co-immunoprecipitate. We conclude that, in yeast, the Npr2/3 complex mediates
an amino acid starvation signal to TORC1.
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