Thomas A. Hall

Works (4)

Updated: July 5th, 2023 16:02

2002 journal article

Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins

RNA, 8(3), 296–306.

By: T. Hall n & J. Brown n

author keywords: archaebacteria; Methanobacterium thermoautotrophicum strain Delta H; Methanothermobacter thermoautotrophicus; ribonuclease P
MeSH headings : Amino Acid Sequence; Animals; Antibody Formation; Blotting, Western; Cell Nucleus / enzymology; Centrifugation, Density Gradient; Cesium / chemistry; Chlorides / chemistry; Chromatography, Affinity; Endoribonucleases / genetics; Endoribonucleases / isolation & purification; Endoribonucleases / metabolism; Eukaryotic Cells / enzymology; Humans; Methanobacterium / enzymology; Molecular Sequence Data; Precipitin Tests; Protein Subunits; RNA, Archaeal / chemistry; RNA, Archaeal / genetics; RNA, Archaeal / metabolism; RNA, Bacterial / metabolism; RNA, Catalytic / genetics; RNA, Catalytic / isolation & purification; RNA, Catalytic / metabolism; RNA, Fungal / genetics; RNA, Fungal / metabolism; Rabbits; Recombinant Proteins / immunology; Recombinant Proteins / isolation & purification; Recombinant Proteins / metabolism; Ribonuclease P; Saccharomyces cerevisiae / enzymology; Sequence Homology, Amino Acid
TL;DR: 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. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

2001 journal article

Characterization of RNAse P holoenzymes from methanococcusjannaschii and methanothermobacter thermoautotrophicus

Biological Chemistry Hoppe-Seyler, 382(8), 1171–1177.

By: A. Andrews, T. Hall & J. Brown

Source: NC State University Libraries
Added: August 6, 2018

2001 chapter

The ribonuclease P family

In Ribonucleases: Pt. A (Vol. 341, pp. 56–77). San Diego, CA: Academic Press.

By: T. Hall & J. Brown

Source: NC State University Libraries
Added: August 6, 2018

1999 journal article

RNase P RNAs from some Archaea are catalytically active

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 96(14), 7803–7808.

By: J. Pannucci n, E. Haas n, T. Hall n, J. Harris n & J. Brown n

MeSH headings : Archaea / enzymology; Archaea / genetics; Bacillus / enzymology; Bacillus / genetics; Base Sequence; Conserved Sequence; Endoribonucleases / chemistry; Endoribonucleases / genetics; Endoribonucleases / metabolism; Kinetics; Methanobacterium / enzymology; Methanobacterium / genetics; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Phylogeny; RNA, Archaeal / chemistry; RNA, Archaeal / genetics; RNA, Archaeal / metabolism; RNA, Bacterial / metabolism; RNA, Catalytic / chemistry; RNA, Catalytic / genetics; RNA, Catalytic / metabolism; Ribonuclease P
TL;DR: The properties of the archaeal RNase P RNAs (high ionic-strength requirement, low affinity for substrate, and catalytic reconstitution by bacterialRNase P protein) are similar to synthetic RNases that contain all of the catalytic core of the bacterial RNA but lack phylogenetically variable, stabilizing elements. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

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