TY - JOUR
T1 - Small nuclear ribonucleoprotein particle assembly in vivo
T2 - Demonstration of a 6S RNA-free core precursor and posttranslational modification
AU - Fisher, David E.
AU - Conner, Gregory E.
AU - Reeves, Westley H.
AU - Wisniewolski, Rosanne
AU - Blobel, Günter
PY - 1985/10
Y1 - 1985/10
N2 - The in vivo synthesis and assembly of human small nuclear ribonucleoproteins (snRNPs) have been studied using pulse/chase analysis. Antibodies derived from patients with systemic lupus erythematosus (SLE) and mixed connective tissue disease (MCTD) recognize distinguishable subsets of pulse-labeled snRNP peptides. These antibodies were used to immunoprecipitate sucrose gradient fractionated pulse-labeled and pulse/chased snRNP proteins. The results indicate that assembly of the U RNA-containing snRNPs is a multistep process involving prior assembly of an RNA-free 6S core particle. This precursor contains snRNP peptides D, E, F, and G, which are common to all the different U RNA-containing particles. Furthermore, a posttranslational modification of one of the U1 snRNP-specific peptides has been observed, and the kinetics of this process indicates that the modification occurs after particle assembly. Functional and structural implications of a protein core for snRNP particles are discussed.
AB - The in vivo synthesis and assembly of human small nuclear ribonucleoproteins (snRNPs) have been studied using pulse/chase analysis. Antibodies derived from patients with systemic lupus erythematosus (SLE) and mixed connective tissue disease (MCTD) recognize distinguishable subsets of pulse-labeled snRNP peptides. These antibodies were used to immunoprecipitate sucrose gradient fractionated pulse-labeled and pulse/chased snRNP proteins. The results indicate that assembly of the U RNA-containing snRNPs is a multistep process involving prior assembly of an RNA-free 6S core particle. This precursor contains snRNP peptides D, E, F, and G, which are common to all the different U RNA-containing particles. Furthermore, a posttranslational modification of one of the U1 snRNP-specific peptides has been observed, and the kinetics of this process indicates that the modification occurs after particle assembly. Functional and structural implications of a protein core for snRNP particles are discussed.
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U2 - 10.1016/0092-8674(85)90271-5
DO - 10.1016/0092-8674(85)90271-5
M3 - Article
C2 - 2932224
AN - SCOPUS:0022133408
VL - 42
SP - 751
EP - 758
JO - Cell
JF - Cell
SN - 0092-8674
IS - 3
ER -