Analysis of conserved positions in nuclear RNase P RNA.
Secondary structure models of eubacterial and eukaryotic nuclear RNase P RNA subunits show extensive structural similarities, allowing the identification of highly conserved nucleotide positions and molecular modeling of the enzyme-substrate complex in three dimensions. Based on this information, we present a preliminary tertiary structure model of the yeast nuclear RNase P RNA. In addition, the most conserved positions in the structure have been subjected to sequence randomization, with viable sequence variations identified by selection in vivo and characterized for phenotypic consequences.
Pagán-Ramos
E
E
Department of Biological Chemistry, University of Michigan, Ann Arbor 40109-0606, USA.
Tranguch
A J
AJ
Nolan
J M
JM
Pace
N R
NR
Engelke
D R
DR
D001483:Base Sequence; D002467:Cell Nucleus / Q000201:enzymology; D017124:Conserved Sequence; D004722:Endoribonucleases / Q000737:chemistry / Q000235:genetics*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009690:Nucleic Acid Conformation; D010641:Phenotype; D016337:RNA, Catalytic / Q000737:chemistry / Q000235:genetics*; D012331:RNA, Fungal / Q000737:chemistry / Q000235:genetics*; D043262:Ribonuclease P; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics
D016337:RNA, Catalytic; D012331:RNA, Fungal; D004722:Endoribonucleases; D043262:Ribonuclease P