Joseph Christopher Ellis

author keywords: ribonuclease P; archaea; rihozyme; Methanothermobacter thermoautotrophicus; Mth1483; Rpp25

MeSH headings : Archaeal Proteins / chemistry; Archaeal Proteins / isolation & purification; Archaeal Proteins / physiology; DNA-Binding Proteins / chemistry; DNA-Binding Proteins / isolation & purification; DNA-Binding Proteins / physiology; Endoribonucleases; Humans; Methanobacteriaceae / enzymology; Protein Subunits / chemistry; Protein Subunits / physiology; RNA, Catalytic; Ribonuclease P / chemistry; Ribonuclease P / isolation & purification; Ribonuclease P / physiology

TL;DR: Using the same biochemical methods used to show that four other proteins homologous to eukaryotic RNase P proteins are bona fideRNase P subunits in Archaea, it is found that there is no evidence that Alba is an RN enzyme P subunit. (via Semantic Scholar)

MeSH headings : Bacteria / metabolism; Base Sequence; Escherichia coli / genetics; Gene Expression Regulation, Bacterial; Genome, Bacterial; Models, Genetic; Molecular Sequence Data; Ribonuclease P / genetics; Ribosomal Proteins / genetics; Thermus thermophilus / genetics

TL;DR: Recently, an unusual gene structure has been described in species of the genus Thermus, in which the rpmH coding sequence was found to be entirely overlapped by the unusually large rnpA (RNase P protein subunit) sequence. (via Semantic Scholar)