Identification of the Ro and La Antigens in the Endoribonuclease VII--ribonucleoprotein Complex

Overview

Journal Biochem J

Specialty Biochemistry

Date 1987 Apr 1

PMID 2440423

Citations 7

Authors

M Bachmann

W J Mayet

H C Schroder

K Pfeifer

K H Meyer zum Buschenfelde

W E Muller

Affiliations

Soon will be listed here.

Abstract

45 S RNP (ribonucleoprotein) particles from calf thymus or L5178y mouse lymphoma cells contain the poly(A)-modulated and oligo(U)-binding endoribonuclease VII [Bachmann, Zahn & Müller (1983) J. Biol. Chem. 258, 7033-7040]. From these particles a 4.5 S RNA was isolated that possesses an oligo(U) sequence. By using monospecific and non-cross-reacting antibodies directed against the La or Ro antigen, both proteins were identified in the endoribonuclease VII-RNP complex after phosphorylation in vitro. In a second approach, endoribonuclease VII activity was identified in immunoaffinity-purified Ro RNPs after preparative isoelectric focusing. Therefore we conclude that the 4.5 S RNA belongs to the Ro RNAs. The results indicate a possible function of endoribonuclease VII in activating stored mRNAs.

Citing Articles

Characterization of murine monoclonal antibodies against 60-kD Ro/SS-A and La/SS-B autoantigens.

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Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes.

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A 52-kD protein is a novel component of the SS-A/Ro antigenic particle.

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The La antigen shuttles between the nucleus and the cytoplasm in CV-1 cells.

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Isolation and characterization of a cDNA clone encoding the 60-kD component of the human SS-A/Ro ribonucleoprotein autoantigen.

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