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Molecular and Cellular Biology, April 2002, p. 2564-2574, Vol. 22, No. 8
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.8.2564-2574.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Novel G-Protein Complex Whose Requirement Is Linked to the Translational Status of the Cell

Anne Carr-Schmid,1 Christine Pfund,2 Elizabeth A. Craig,2 and Terri Goss Kinzy1,3*

Department of Molecular Genetics and Microbiology, UMDNJ Robert Wood Johnson Medical School,1 The Cancer Institute of New Jersey, Piscataway, New Jersey 08854,3 Department of Biomolecular Chemistry, University of Wisconsin—Madison, Madison, Wisconsin 537062

Received 15 October 2001/ Returned for modification 14 November 2001/ Accepted 11 January 2002

G proteins, which bind and hydrolyze GTP, are involved in regulating a variety of critical cellular processes, including the process of protein synthesis. Many members of the subfamily of elongation factor class G proteins interact with the ribosome and function to regulate discrete steps during the process of protein synthesis. Despite sequence similarity to factors involved in translation, a role for the yeast Hbs1 protein has not been defined. In this work we have identified a genetic relationship between genes encoding components of the translational apparatus and HBS1. HBS1, while not essential for viability, is important for efficient growth and protein synthesis under conditions of limiting translation initiation. The identification of an Hbs1p-interacting factor, Dom34p, which shares a similar genetic relationship with components of the translational apparatus, suggests that Hbs1p and Dom34p may function as part of a complex that facilitates gene expression. Dom34p contains an RNA binding motif present in several ribosomal proteins and factors that regulate translation of specific mRNAs. Thus, Hbs1p and Dom34p may function together to help directly or indirectly facilitate the expression either of specific mRNAs or under certain cellular conditions.

* Corresponding author. Mailing address: Department of Molecular Genetics and Microbiology, UMDNJ Robert Wood Johnson Medical School, 675 Hoes Ln., Piscataway, NJ 08854-5635. Phone: (732)235-5450. Fax: (732)235-5223. E-mail: kinzytg{at}umdnj.edu.

Molecular and Cellular Biology, April 2002, p. 2564-2574, Vol. 22, No. 8
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.8.2564-2574.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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