A subunit of human nuclear RNase P has ATPase activity.
Human nuclear RNase P purified from HeLa cells has ATPase activity. This activity is associated with one of the protein subunits of the enzyme, Rpp20. Thus, human nuclear RNase P, which contains several proteins and one essential RNA, has at least one other enzymatic activity in addition to cleavage of phosphoester bonds in RNA. The amino acid sequence of Rpp20 has a signature motif found in an ATPase-containing subunit of a family of protein complexes (ABC transporters) that mediate a variety of trans-membrane traffic, as well as a segment, DIxxN, that resembles the DEAD box motif of many ATPases: together, these might represent an ATPase signature motif.
Li
Y
Y
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
Altman
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S
D000255:Adenosine Triphosphate / Q000378:metabolism*; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D004722:Endoribonucleases / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins; D006367:HeLa Cells / Q000201:enzymology; D020035:Holoenzymes / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009363:Neoplasm Proteins / Q000737:chemistry / Q000378:metabolism; D021122:Protein Subunits; D016337:RNA, Catalytic / Q000737:chemistry / Q000378:metabolism*; D043262:Ribonuclease P; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D020035:Holoenzymes; D009363:Neoplasm Proteins; D021122:Protein Subunits; D016337:RNA, Catalytic; D000255:Adenosine Triphosphate; D004722:Endoribonucleases; C468368:RPP14 protein, human; D043262:Ribonuclease P; C470865:ribonuclease P, E coli