TY - JOUR
T1 - Autoantigenic properties of some protein subunits of catalytically active complexes of human ribonuclease P
AU - Jarrous, Nayef
AU - Eder, Paul S.
AU - Guerrier-Takada, Cecilia
AU - Hoog, Christer
AU - Altman, Sidney
PY - 1998/4
Y1 - 1998/4
N2 - At least six proteins co-purify with human ribonuclease P (RNase P), a tRNA processing ribonucleoprotein. Two of these proteins, Rpp30 and Rpp38, are Th autoantigens. Recombinant Rpp30 and Rpp38 are also recognized by Th sera from systemic sclerosis patients. Two of the other proteins associated with RNase P, Rpp20 and Rpp40, do not cross-react with Th sera. Polyclonal antibodies raised against all four recombinant proteins recognize the corresponding proteins associated with RNase P and precipitate active holoenzyme. Catalytically active RNase P holoenzyme can be separated from the nucleolar and mitochondrial RNA processing endoribonuclease, RNase MRP, even though these two enzymes may share some subunits.
AB - At least six proteins co-purify with human ribonuclease P (RNase P), a tRNA processing ribonucleoprotein. Two of these proteins, Rpp30 and Rpp38, are Th autoantigens. Recombinant Rpp30 and Rpp38 are also recognized by Th sera from systemic sclerosis patients. Two of the other proteins associated with RNase P, Rpp20 and Rpp40, do not cross-react with Th sera. Polyclonal antibodies raised against all four recombinant proteins recognize the corresponding proteins associated with RNase P and precipitate active holoenzyme. Catalytically active RNase P holoenzyme can be separated from the nucleolar and mitochondrial RNA processing endoribonuclease, RNase MRP, even though these two enzymes may share some subunits.
KW - Auto-antigens
KW - Human RNase P
KW - Nuclear localization sequences
KW - RNase MRP
UR - http://www.scopus.com/inward/record.url?scp=0031900726&partnerID=8YFLogxK
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C2 - 9630247
AN - SCOPUS:0031900726
SN - 1355-8382
VL - 4
SP - 407
EP - 417
JO - RNA
JF - RNA
IS - 4
ER -