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

Published online by Cambridge University Press:  07 February 2001

XING-WANG FANG
Affiliation:
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA
XIAO-JING YANG
Affiliation:
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA
KENNETH LITTRELL
Affiliation:
Argonne National Laboratory, Argonne, IL 60439, USA
S. NIRANJANAKUMARI
Affiliation:
Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA
P. THIYAGARAJAN
Affiliation:
Argonne National Laboratory, Argonne, IL 60439, USA
CAROL A. FIERKE
Affiliation:
Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA
TOBIN R. SOSNICK
Affiliation:
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA
TAO PAN
Affiliation:
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA
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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.

Type
Research Article
Copyright
2001 RNA Society

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