@article{harris_haas_williams_frank_brown_2001, title={New insight into RNase P RNA structure from comparative analysis of the archaeal RNA}, volume={7}, ISSN={["1469-9001"]}, DOI={10.1017/S1355838201001777}, abstractNote={A detailed comparative analysis of archaeal RNase P RNA structure and a comparison of the resulting structural information with that of the bacterial RNA reveals that the archaeal RNase P RNAs are strikingly similar to those of Bacteria. The differences between the secondary structure models of archaeal and bacterial RNase P RNA have largely disappeared, and even variation in the sequence and structure of the RNAs are similar in extent and type. The structure of the cruciform (P7-11) has been reevaluated on the basis of a total of 321 bacterial and archaeal sequences, leading to a model for the structure of this region of the RNA that includes an extension to P11 that consistently organizes the cruciform and adjacent highly-conserved sequences.}, number={2}, journal={RNA}, author={Harris, JK and Haas, ES and Williams, D and Frank, DN and Brown, JW}, year={2001}, month={Feb}, pages={220–232} }
 @article{pannucci_haas_hall_harris_brown_1999, title={RNase P RNAs from some Archaea are catalytically active}, volume={96}, ISSN={["0027-8424"]}, DOI={10.1073/pnas.96.14.7803}, abstractNote={
            The RNA subunits of RNase Ps of Archaea and eukaryotes have been thought to depend fundamentally on protein for activity, unlike those of Bacteria that are capable of efficient catalysis in the absence of protein. Although the eukaryotic RNase P RNAs are quite different than those of Bacteria in both sequence and structure, the archaeal RNAs generally contain the sequences and structures of the bacterial, phylogenetically conserved catalytic core. A spectrum of archaeal RNase P RNAs were therefore tested for activity in a wide range of conditions. Many remain inactive in ionically extreme conditions, but catalytic activity could be detected from those of the methanobacteria, thermococci, and halobacteria. Chimeric holoenzymes, reconstituted from the
            Methanobacterium
            RNase P RNA and the
            Bacillus subtilis
            RNase P protein subunits, were functional at low ionic strength. The properties of the archaeal RNase P RNAs (high ionic-strength requirement, low affinity for substrate, and catalytic reconstitution by bacterial RNase P protein) are similar to synthetic RNase P RNAs that contain all of the catalytic core of the bacterial RNA but lack phylogenetically variable, stabilizing elements.
          }, number={14}, journal={PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA}, author={Pannucci, JA and Haas, ES and Hall, TA and Harris, JK and Brown, JW}, year={1999}, month={Jul}, pages={7803–7808} }
 @article{haas_brown_1998, title={Evolutionary variation in bacterial RNase P RNAs}, volume={26}, ISSN={["0305-1048"]}, DOI={10.1093/nar/26.18.4093}, abstractNote={Sequences encoding RNase P RNAs from representatives of the last remaining classical phyla of Bacteria have been determined, completing a general phylogenetic survey of RNase P RNA sequence and structure. This broad sampling of RNase P RNAs allows some refinement of the secondary structure, and reveals patterns in the evolutionary variation of sequences and secondary structures. Although the sequences range from 100 to <25% identical to one another, and although only 40 of the nucleotides are invariant, there is considerable conservation of the underlying core of the RNA sequence. RNase P RNAs, like group I intron RNAs but unlike ribosomal RNAs, transfer RNAs or other highly conserved RNAs, are quite variable in secondary structure outside of this conserved structural core. Conservative regions of the RNA evolve by substitution of apparently interchangeable alternative structures, rather than the insertion and deletion of helical elements that occurs in the more variable regions of the RNA. In a remarkable case of convergent molecular evolution, most of the unusual structural elements of type B RNase P RNAs of the low G+C Gram-positive Bacteria have evolved independently in Thermomicrobium roseum , a member of the green non-sulfur Bacteria.}, number={18}, journal={NUCLEIC ACIDS RESEARCH}, author={Haas, ES and Brown, JW}, year={1998}, month={Sep}, pages={4093–4099} }
 @article{selvamurugan_joost_haas_brown_galvin_eliceiri_1997, title={Intracellular localization and unique conserved sequences of three small nucleolar RNAs}, volume={25}, ISSN={["0305-1048"]}, DOI={10.1093/nar/25.8.1591}, abstractNote={Three human small nucleolar RNAs (snoRNAs), E1, E2 and E3, were reported earlier that have unique sequences, interact directly with unique segments of pre-rRNA in vivo and are encoded in introns of protein genes. In the present report, human and frog E1, E2 and E3 RNAs injected into the cytoplasm of frog oocytes migrated to the nucleus and specifically to the nucleolus. This indicates that the nucleolar and nuclear localization signals of these snoRNAs reside within their evolutionarily conserved segments. Homologs of these snoRNAs from several vertebrates were sequenced and this information was used to develop RNA secondary structure models. These snoRNAs have unique phylogenetically conserved sequences.}, number={8}, journal={NUCLEIC ACIDS RESEARCH}, author={Selvamurugan, N and Joost, OH and Haas, ES and Brown, JW and Galvin, NJ and Eliceiri, GL}, year={1997}, month={Apr}, pages={1591–1596} }