Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III.

Journal article

RNA polymerases are essential enzymes which transcribe DNA into RNA. Here, we obtain mass spectra of the cellular forms of apo and holo eukaryotic RNA polymerase I and III, defining their composition under different solution conditions. By recombinant expression of subunits within the initiation heterotrimer of Pol III, we derive an interaction network and couple this data with ion mobility data to define topological restraints. Our data agree with available structural information and homolog...

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Authors: Lane, L; Fernández-Tornero, C; Zhou, M; Morgner, N; Ptchelkine, D

• Publication status: Published
• Journal: Structure (London, England : 1993)
• Volume: 19
• Issue: 1
• Pages: 90-100
• Publication date: 2011-01-01
• DOI: 10.1016/j.str.2010.11.009
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English
• Keywords: Protein Structure, Quaternary; Spectrometry, Mass, Electrospray Ionization; RNA Polymerase I; Saccharomyces cerevisiae Proteins; Polydeoxyribonucleotides; Saccharomyces cerevisiae; Protein Stability; RNA Polymerase III; Protein Multimerization; Apoenzymes; Protein Structure, Tertiary