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

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Published inEukaryotic Cell Vol. 2; no. 5; pp. 1046 - 1052
Main Authors Naryshkina, Tatyana, Bruning, Adrian, Gadal, Olivier, Severinov, Konstantin
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.10.2003
Subjects
Amino Acid Sequence
Amino Acid Substitution
Cell Division - drug effects
Cell Division - genetics
Cell Nucleolus - chemistry
Galactose - pharmacology
Glucose - pharmacology
Microscopy, Fluorescence
Molecular Sequence Data
Mutagenesis, Site-Directed
Protein Binding
Protein Structure, Quaternary
Protein Subunits - genetics
Protein Subunits - metabolism
Protein Subunits - physiology
RNA Polymerase I - chemistry
RNA Polymerase I - genetics
RNA Polymerase I - metabolism
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - physiology
Transformation, Genetic
Zinc - metabolism
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Abstract Classifications Services EC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue EC About EC Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy EC RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 1535-9778 Online ISSN: 1535-9786 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to EC .asm.org, visit: EC       
AbstractList The second-largest subunits of eukaryal RNA polymerases are similar to the beta 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 Zn(2+) 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.
The second-largest subunits of eukaryal RNA polymerases are similar to the beta 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 Zn super(2+) 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.
The second-largest subunits of eukaryal RNA polymerases are similar to the β 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 Zn 2+ 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.
Classifications Services EC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue EC About EC Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy EC RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 1535-9778 Online ISSN: 1535-9786 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to EC .asm.org, visit: EC       
ABSTRACT The second-largest subunits of eukaryal RNA polymerases are similar to the β 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 Zn 2+ 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.
Author Konstantin Severinov
Adrian Bruning
Olivier Gadal
Tatyana Naryshkina
AuthorAffiliation 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, France 2
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Corresponding author. Mailing address: Waksman Institute, 190 Frelinghuysen Rd., Piscataway, NJ 08854. Phone: (732) 445-6095. Fax: (732) 445-5735. E-mail: severik@waksman.rutgers.edu.
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Snippet Classifications Services EC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit...
The second-largest subunits of eukaryal RNA polymerases are similar to the beta subunits of prokaryal RNA polymerases throughout much of their lengths. The...
ABSTRACT The second-largest subunits of eukaryal RNA polymerases are similar to the β subunits of prokaryal RNA polymerases throughout much of their lengths....
The second-largest subunits of eukaryal RNA polymerases are similar to the β subunits of prokaryal RNA polymerases throughout much of their lengths. The...
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SubjectTerms Amino Acid Sequence
Amino Acid Substitution
Cell Division - drug effects
Cell Division - genetics
Cell Nucleolus - chemistry
Galactose - pharmacology
Glucose - pharmacology
Microscopy, Fluorescence
Molecular Sequence Data
Mutagenesis, Site-Directed
Protein Binding
Protein Structure, Quaternary
Protein Subunits - genetics
Protein Subunits - metabolism
Protein Subunits - physiology
RNA Polymerase I - chemistry
RNA Polymerase I - genetics
RNA Polymerase I - metabolism
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - physiology
Transformation, Genetic
Zinc - metabolism
Title Role of Second-Largest RNA Polymerase I Subunit Zn-Binding Domain in Enzyme Assembly
URI http://ec.asm.org/content/2/5/1046.abstract
https://www.ncbi.nlm.nih.gov/pubmed/14555487
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