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Eukaryotic Cell, October 2003, p. 1046-1052, Vol. 2, No. 5
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.5.1046-1052.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Role of Second-Largest RNA Polymerase I Subunit Zn-Binding Domain in Enzyme Assembly

Tatyana Naryshkina,1 Adrian Bruning,1 Olivier Gadal,2 and Konstantin Severinov1,3*

Waksman Institute,1 Department of Molecular Biology and Biochemistry, Rutgers, The State University, Piscataway, NJ 08854,3 Unité de Biologie Cellulaire du Noyau, CNRS URA 1773, 75724 Paris cedex 165, France2

Received 18 May 2003/ Accepted 26 July 2003

The second-largest subunits of eukaryal RNA polymerases are similar to the ß subunits of prokaryal RNA polymerases throughout much of their lengths. The second-largest subunits from eukaryal RNA polymerases contain a four-cysteine Zn-binding domain at their C termini. The domain is also present in archaeal homologs but is absent from prokaryal homologs. Here, we investigated the role of the C-terminal Zn-binding domain of Rpa135, the second-largest subunit of yeast RNA polymerase I. Analysis of nonfunctional Rpa135 mutants indicated that the Zn-binding domain is required for recruitment of the largest subunit, Rpa190, into the RNA polymerase I complex. Curiously, the essential function of the Rpa135 Zn-binding domain is not related to Zn2+ binding per se, since replacement of only one of the four cysteine residues with alanine led to the loss of Rpa135 function. Even more strikingly, replacement of all four cysteines with alanines resulted in functional Rpa135.

* Corresponding author. Mailing address: Waksman Institute, 190 Frelinghuysen Rd., Piscataway, NJ 08854. Phone: (732) 445-6095. Fax: (732) 445-5735. E-mail: severik{at}waksman.rutgers.edu.

Eukaryotic Cell, October 2003, p. 1046-1052, Vol. 2, No. 5
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.5.1046-1052.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.





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