@article{hall_brown_2002, title={Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins}, volume={8}, ISSN={["1469-9001"]}, DOI={10.1017/S1355838202028492}, abstractNote={Although archaeal RNase P RNAs are similar in both sequence and structure to those of Bacteria rather than eukaryotes, and heterologous reconstitution between the Bacillus subtilis RNase P protein and some archaeal RNase P RNAs has been demonstrated, no archaeal protein sequences with similarity to any known bacterial RNase P protein subunit have been identified, and the density of Methanothermobacter thermoautotrophicus RNase P in Cs2SO4 (1.42 g/mL) is inconsistent with a single small bacterial-like protein subunit. Four hypothetical open reading frames (MTH11, MTH687, MTH688, and MTH1618) were identified in the genome of M. thermoautotrophicus that have sequence similarity to four of the nine Saccharomyces cerevisiae RNase P protein subunits: Pop4p, Pop5p, Rpp1p, and Rpr2p, respectively. Polyclonal antisera generated to recombinant Mth11p, Mth687p, Mth688p, and Mth1618p each recognized a protein of the predicted molecular weight in western blots of partially purified M. thermoautotrophicus RNase P, and immunoprecipitated RNase P activity from the same partially purified preparation. RNase P in Archaea is therefore composed of an RNA subunit similar to bacterial RNase P RNA and multiple protein subunits similar to those in the eukaryotic nucleus.}, number={3}, journal={RNA}, author={Hall, TA and Brown, JW}, year={2002}, month={Mar}, pages={296–306} }
 @article{andrews_hall_brown_2001, title={Characterization of RNAse P holoenzymes from methanococcusjannaschii and methanothermobacter thermoautotrophicus}, volume={382}, number={8}, journal={Biological Chemistry Hoppe-Seyler}, author={Andrews, A. J. and Hall, T. A. and Brown, J. W.}, year={2001}, pages={1171–1177} }
 @inbook{hall_brown_2001, title={The ribonuclease P family}, volume={341}, booktitle={Ribonucleases: Pt. A}, publisher={San Diego, CA: Academic Press}, author={Hall, T. A. and Brown, J. W.}, year={2001}, pages={56–77} }
 @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} }