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Updated: Feb 17, 2026

Temporal Quantification of MAPK Induced Expression in Single Yeast Cells
Published on: October 4, 2013
MPK1/SLT2 Links Multiple Stress Responses with Gene Expression in Budding Yeast by Phosphorylating Tyr1 of the RNAP
Nathan Yurko1, Xiaochuan Liu2, Takashi Yamazaki1
1Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
Abstract:
The RNA polymerase II largest subunit C-terminal domain consists of repeated YSPTSPS heptapeptides. The role of tyrosine-1 (Tyr1) remains incompletely understood, as, for example, mutating all Tyr1 residues to Phe (Y1F) is lethal in vertebrates but a related mutant has only a mild phenotype in S. pombe. Here we show that Y1F substitution in budding yeast resulted in a strong slow-growth phenotype. The Y1F strain was also hypersensitive to several different cellular stresses that involve MAP kinase signaling. These phenotypes were all linked to transcriptional changes, and we also identified genetic and biochemical interactions between Tyr1 and both transcription initiation and termination factors. Further studies uncovered defects related to MAP kinase I (Slt2) pathways, and we provide evidence that Slt2 phosphorylates Tyr1 in vitro and in vivo. Our study has thus identified Slt2 as a Tyr1 kinase, and in doing so provided links between stress response activation and Tyr1 phosphorylation.
Insights
The study reveals that substituting tyrosine-1 (Tyr1) in RNA polymerase II
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- The C-terminal domain of RNA polymerase II's largest subunit features YSPTSPS repeats.
- The function of tyrosine-1 (Tyr1) in this domain is not fully understood.
- Previous studies show varied effects of Tyr1 mutations across species.
Purpose of the Study:
- To investigate the role of Tyr1 in budding yeast.
- To explore the connection between Tyr1, cellular stress, and MAP kinase signaling.
- To identify the kinase responsible for Tyr1 phosphorylation.
Main Methods:
- Generating and analyzing a Tyr1 to Phenylalanine (Y1F) mutant in budding yeast.
- Assessing growth phenotypes and stress sensitivity.
- Investigating transcriptional changes and genetic/biochemical interactions.
- Performing in vitro and in vivo phosphorylation assays.
Main Results:
- The Y1F mutation caused slow growth and hypersensitivity to cellular stresses.
- Phenotypes were associated with transcriptional alterations.
- Genetic and biochemical interactions between Tyr1 and transcription factors were observed.
- The MAP kinase Slt2 was identified as a Tyr1 kinase, phosphorylating Tyr1 in vitro and in vivo.
Conclusions:
- Tyr1 phosphorylation by Slt2 is crucial for budding yeast.
- This finding links stress response pathways to Tyr1 function in RNA polymerase II.
- The study elucidates a novel regulatory mechanism for transcription.
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