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Solution structure of the hRPABC14.4 subunit of human RNA polymerases

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Abstract

The protein hRPABC14.4 is an essential subunit of human RNA polymerases I, II, and III and is required for the transcription of all human nuclear genes. The structure of hRPABC14.4 was determined by nuclear magnetic resonance spectroscopy. The protein fold comprises a highly conserved central domain forming two antiparallel α-helices flanked by the less conserved N- and C-terminal regions forming a five-stranded β-sandwich. Amino acids from the two helices participate in the generation of a hydrophobic surface area which is conserved in all eukaryotic and archaeal homologous subunits, and likely constitutes a critical macromolecular interaction interface. The hRPABC14.4 structure accounts for mutagenesis results in Saccharomyces cerevisiae and provides a structural working model for elucidating the role of this subunit in the molecular architecture and function of the human nuclear RNA polymerases.

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Figure 2: Solution structure of hRPABC14.4.
Figure 1: Sequence alignment of hRPABC14.4 with homologous proteins.
Figure 3: Charge distribution at the surface of hRPABC14.4.
Figure 4: Sequence conservation and mutational data.

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Acknowledgements

Supported by grants from the American Heart Association and National Institutes of Health (J.A.A.L.), and grants from the National Institutes of Health and National Science Foundation (G.W.). J.A.A.L. is an Established Investigator of the American Heart Association.

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Author notes

  1. Federico del Río-Portilla

    Present address: Institute of Chemistry, National University of Mexico, 04350, Mexico, D. F., Mexico

  2. Dara Gilbert

    Present address: Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, California, 90024, USA

Authors and Affiliations

  1. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, 02115, Massachusetts, USA

    Federico del Río-Portilla, Dara Gilbert & Gerhard Wagner

  2. Department of Medicine, Gene Regulation Laboratory and Macromolecular Crystallography Unit, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, 02115, Massachusetts, USA

    Andrew Gaskell & John A. A. Ladias

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  1. Federico del Río-Portilla
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Correspondence to Gerhard Wagner.

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del Río-Portilla, F., Gaskell, A., Gilbert, D. et al. Solution structure of the hRPABC14.4 subunit of human RNA polymerases. Nat Struct Mol Biol 6, 1039–1042 (1999). https://doi.org/10.1038/14923

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