The largest subunit of human RNA polymerase III is closely related to the largest subunit of yeast and trypanosome RNA polymerase III

Sepehri, S., Hernandez, N. (1997) The largest subunit of human RNA polymerase III is closely related to the largest subunit of yeast and trypanosome RNA polymerase III. Genome Research, 7 (10). pp. 1006-19. ISSN 1088-9051

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URL: http://www.ncbi.nlm.nih.gov/pubmed/9331371
DOI: 10.1101/gr.7.10.1006

Abstract

In both yeast and mammalian systems, considerable progress has been made toward the characterization of the transcription factors required for transcription by RNA polymerase III. However, whereas in yeast all of the RNA polymerase III subunits have been cloned, relatively little is known about the enzyme itself in higher eukaryotes. For example, no higher eukaryotic sequence corresponding to the largest RNA polymerase III subunit is available. Here we describe the isolation of cDNAs that encode the largest subunit of human RNA polymerase III, as suggested by the observations that (1) antibodies directed against the cloned protein immunoprecipitate an active enzyme whose sensitivity to different concentrations of alpha-amanitin is that expected for human RNA polymerase III; and (2) depletion of transcription extracts with the same antibodies results in inhibition of transcription from an RNA polymerase III, but not from an RNA polymerase II, promoter. Sequence comparisons reveal that regions conserved in the RNA polymerase I, II, and III largest subunits characterized so far are also conserved in the human RNA polymerase III sequence, and thus probably perform similar functions for the human RNA polymerase III enzyme.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals Antibody Specificity Cell-Free System Cloning, Molecular Comparative Study Conserved Sequence Evolution, Molecular Humans Molecular Sequence Data Precipitin Tests Protein Conformation RNA Polymerase III/classification/ genetics/immunology/isolation & purification Recombinant Proteins/isolation & purification Research Support, U.S. Gov't, P.H.S. Saccharomyces cerevisiae/enzymology/genetics Sequence Homology, Amino Acid Species Specificity Transcription, Genetic Trypanosoma brucei brucei/enzymology/genetics
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > RNA polymerase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > antibodies
evolution
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Hernandez lab
Depositing User: Kathleen Darby
Date: October 1997
Date Deposited: 07 May 2014 16:08
Last Modified: 07 May 2014 16:08
PMCID: PMC310672
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30014

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