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Eukaryotic Cell, January 2005, p. 82-89, Vol. 4, No. 1
1535-9778/05/$08.00+0     doi:10.1128/EC.4.1.82-89.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Broad Sensitivity of Saccharomyces cerevisiae Lacking Ribosome-Associated Chaperone Ssb or Zuo1 to Cations, Including Aminoglycosides

So-Young Kim{dagger} and Elizabeth A. Craig*

Department of Biochemistry, University of Wisconsin—Madison, Madison, Wisconsin

Received 14 October 2004/ Accepted 5 November 2004

The Hsp70 Ssb and J protein Zuo1 of Saccharomyces cerevisiae are ribosome-associated molecular chaperones, proposed to be involved in the folding of newly synthesized polypeptide chains. Cells lacking Ssb and/or Zuo1 have been reported to be hypersensitive to cationic aminoglycoside protein synthesis inhibitors that affect translational fidelity and to NaCl. Since we found that {Delta}ssb1 {Delta}ssb2 ({Delta}ssb1,2), {Delta}zuo1, and wild-type cells have very similar levels of translational misreading in the absence of aminoglycosides, we asked whether the sensitivities to aminoglycosides and NaCl represent a general increase in sensitivity to cations. We found that {Delta}ssb1,2 and {Delta}zuo1 cells are hypersensitive to a wide range of cations. This broad sensitivity is similar to that of cells having lowered activity of major plasma membrane transporters, such as the major K+ transporters Trk1 and Trk2 or their regulators Hal4 and Hal5. Like {Delta}hal4,5 cells, {Delta}ssb1,2 and {Delta}zuo1 cells have increased intracellular levels of Na+ and Li+ upon challenge with higher-than-normal levels of these cations, due to an increased rate of influx. In the presence of aminoglycosides, {Delta}ssb1,2, {Delta}zuo1, and {Delta}hal 4,5 cells have similarly increased levels of translational misreading. We conclude that, in vivo, the major cause of the aminoglycoside sensitivity of cells lacking ribosome-associated molecular chaperones is a general increase in cation influx, perhaps due to altered maturation of membrane proteins.


* Corresponding author. Mailing address: 433 Babcock Dr., Department of Biochemistry, University of Wisconsin—Madison, Madison, WI 53706. Phone: (608) 263-7105. Fax: (608) 262-3453. E-mail: ecraig{at}wisc.edu.

{dagger} Present address: Research and Development Center of Bioproducts, CJ Corporation, Ichon-Si, South Korea.


Eukaryotic Cell, January 2005, p. 82-89, Vol. 4, No. 1
1535-9778/05/$08.00+0     doi:10.1128/EC.4.1.82-89.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




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