Autoantigenic properties of some protein subunits of catalytically active complexes of human ribonuclease P.
RNA
; 4(4): 407-17, 1998 Apr.
Article
de En
| MEDLINE
| ID: mdl-9630247
ABSTRACT
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.
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Ribonucléoprotéines
/
Autoantigènes
/
Protéines de transport
/
ARN catalytique
/
Endoribonucleases
Limites:
Humans
Langue:
En
Journal:
RNA
Sujet du journal:
BIOLOGIA MOLECULAR
Année:
1998
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique