title: Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3.
abstract: Ribonuclease P (RNase P) is a ubiquitous trans-acting ribozyme that processes the 5' leader sequence of precursor tRNA (pre-tRNA). The RNase P RNA (PhopRNA) of the hyperthermophilic archaeon Pyrococcus horikoshii OT3 is central to the catalytic process and binds five proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) which contribute to the enzymatic activity of the holoenzyme. Despite significant progress in determining the crystal structure of the proteins, the structure of PhopRNA remains elusive. Comparative analysis of the RNase P RNA sequences and existing crystallographic structural information of the bacterial RNase P RNAs were combined to generate a phylogenetically supported three-dimensional (3-D) model of the PhopRNA. The model structure shows an essentially flat disk with 16 tightly packed helices and a conserved face suitable for the binding of pre-tRNA. Moreover, the structure in solution was investigated by enzymatic probing and small-angle X-ray scattering (SAXS) analysis. The low resolution model derived from SAXS and the comparative 3-D model have similar overall shapes. The 3-D model provides a framework for a better understanding of structure-function relationships of this multifaceted primordial ribozyme.
authors.affiliation: Department of Biochemistry, University of Texas Health Science Center at San Antonio San Antonio, TX 78229-3900, USA.
authors.forename: Christian
authors.initials: C
authors.lastname: Zwieb
authors.forename: Yuji
authors.initials: Y
authors.lastname: Nakao
authors.forename: Takashi
authors.initials: T
authors.lastname: Nakashima
authors.forename: Hisanori
authors.initials: H
authors.lastname: Takagi
authors.forename: Shuichiro
authors.initials: S
authors.lastname: Goda
authors.forename: Ebbe Sloth
authors.initials: ES
authors.lastname: Andersen
authors.forename: Yoshimitsu
authors.initials: Y
authors.lastname: Kakuta
authors.forename: Makoto
authors.initials: M
authors.lastname: Kimura
mesh_terms: D019843:Archaeal Proteins / Q000235:genetics*; D001483:Base Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D019642:RNA, Archaeal / Q000737:chemistry*; D043262:Ribonuclease P / Q000235:genetics*; D053838:Scattering, Small Angle
chemical_list: D019843:Archaeal Proteins; D019642:RNA, Archaeal; D043262:Ribonuclease P