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Vol. 13, Issue 3, 795-804, March 2002
Department of Molecular Biology, University of Texas Southwestern
Medical Center, Dallas, Texas 75390-9148
An important function of the RTG signaling pathway
is maintenance of intracellular glutamate supplies in yeast cells with dysfunctional mitochondria. Herein, we report that MKS1
is a negative regulator of the RTG pathway, acting
between Rtg2p, a proximal sensor of mitochondrial function, and the
bHLH transcription factors Rtg1p and Rtg3p. In mks1
cells, RTG target gene expression is constitutive,
bypassing the requirement for Rtg2p, and is no longer repressible by
glutamate. We show further that Mks1p is a phosphoprotein whose
phosphorylation pattern parallels that of Rtg3p in response to
activation of the RTG pathway, and that Mks1p is in a
complex with Rtg2p. MKS1 was previously implicated in
the formation of [URE3], an inactive prion form of a negative
regulator of the nitrogen catabolite repression pathway, Ure2p.
rtg mutations induce [URE3] and can do so
independently of MKS1. We find that glutamate suppresses
[URE3] formation, suggesting that the Mks1p effect on the formation
of [URE3] can occur indirectly via regulation of the
RTG pathway.
Corresponding author. E-mail: butow{at}swmed.edu.
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