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Molecular and Cellular Biology, November 2005, p. 9753-9763, Vol. 25, No. 22
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.22.9753-9763.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

p38 Mitogen-Activated Protein Kinase/Hog1p Regulates Translation of the AU-Rich-Element-Bearing MFA2 Transcript

Shobha Vasudevan,{dagger} Nicole Garneau, Danny Tu Khounh, and Stuart W. Peltz*

Department of Molecular Genetics, Microbiology and Immunology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School and Rutgers University, 675 Hoes Lane, Piscataway, New Jersey 08854

Received 10 May 2005/ Returned for modification 10 June 2005/ Accepted 29 August 2005

AU-rich-element (ARE)-mediated mRNA regulation occurs in Saccharomyces cerevisiae in response to external and internal stimuli through the p38 mitogen-activated protein kinase (MAPK)/Hog1p pathway. We demonstrate that the ARE-bearing MFA2 3' untranslated region (UTR) controls translation efficiency in a p38 MAPK/Hog1p-dependent manner in response to carbon source growth conditions. The carbon source-regulated effect on MFA2 3'-UTR-controlled translation involves the role of conserved ARE binding proteins, the ELAV/TIA-1-like Pub1p, which can interact with the cap/eIF4G complex, and the translation/mRNA stability factor poly(A) binding protein (Pab1p). Pub1p binds the MFA2 3'-UTR in a p38 MAPK/Hog1p-regulated manner in response to carbon source growth conditions. Significantly, the p38 MAPK/Hog1p is also required to modulate Pab1p in response to carbon source. We find that Pab1p can bind the MFA2 3'-UTR in a regulated manner to control MFA2 3'-UTR reporter translation. Binding of full-length Pab1p to the MFA2 3'-UTR correlates with translation repression. Importantly, Pab1p binds the MFA2 3'-UTR only in a PUB1 strain, and correlating with this requirement, Pub1p controls translation repression of MFA2 in a carbon source/Hog1p-regulated manner. These results suggest that the p38 MAPK/Hog1p pathway regulates 3'-UTR-mediated translation by modulating recruitment of Pab1p and Pub1p, which can interact with the translation machinery.

* Corresponding author. Mailing address: Department of Molecular Genetics, Microbiology and Immunology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School and Rutgers University, 675 Hoes Lane, Piscataway, NJ 08854. Phone: (908) 222-7000. Fax: (908) 222-0567. E-mail: speltz{at}ptcbio.com.

{dagger} Present address: Yale University, 295 Congress Avenue, BCMM 133, New Haven, CT 06519.

Molecular and Cellular Biology, November 2005, p. 9753-9763, Vol. 25, No. 22
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.22.9753-9763.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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