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The Bacillus subtilis RNase P holoenzyme contains two RNase P RNA and two RNase P protein subunits

  • XING-WANG FANG (a1), XIAO-JING YANG (a1), KENNETH LITTRELL (a2), S. NIRANJANAKUMARI (a3), P. THIYAGARAJAN (a2), CAROL A. FIERKE (a3), TOBIN R. SOSNICK (a1) and TAO PAN (a1)...
    • Published online: 07 February 2001
Abstract

Ribonuclease P (RNase P) catalyzes the 5′ maturation of precursor tRNA transcripts and, in bacteria, is composed of a catalytic RNA and a protein. We investigated the oligomerization state and the shape of the RNA alone and the holoenzyme of Bacillus subtilis RNase P in the absence of substrate by synchrotron small-angle X-ray scattering and affinity retention. The B. subtilis RNase P RNA alone is a monomer; however, the scattering profile changes upon the addition of monovalent ions, possibly suggesting different interdomain angles. To our surprise, the X-ray scattering data combined with the affinity retention results indicate that the holoenzyme contains two RNase P RNA and two RNase P protein molecules. We propose a structural model of the holoenzyme with a symmetrical arrangement of the two RNA subunits, consistent with the X-ray scattering results. This (P RNA)2(P protein)2 complex likely binds substrate differently than the conventional (P RNA)1(P protein)1 complex; therefore, the function of the B. subtilis RNase P holoenzyme may be more diverse than previously thought. These revisions to our knowledge of the RNase P holoenzyme suggest a more versatile role for proteins in ribonucleoprotein complexes.

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Corresponding author
Reprint requests to: Tao Pan, Department of Biochemistry and Molecular Biology, University of Chicago, 920 East 58th Street, Chicago, Illinois 60637, USA; e-mail: taopan@midway.uchicago.edu.
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RNA
  • ISSN: 1355-8382
  • EISSN: 1469-9001
  • URL: /core/journals/rna
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