Skip Navigation

This Article
Right arrow Print PDF (4451K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Rosa, M. D.
Right arrow Articles by Reichlin, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rosa, M. D.
Right arrow Articles by Reichlin, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1983, Vol. 11, No. 3 853-870
© 1983

MOLECULAR BIOLOGY

A mammalian tRNA His-Containing antigen is recognized by the polymyosits-specific antibody antijo-1

Margaret D. Rosa*,, Joseph P. Hendrick, Jr.**,, Michael R. Lerner+,, Joan A. Steitz and Morris Reichlin

Department of Molecular Biophysics and Biochemistry, Yale University Yale University, New Haven, CT 06510, USA Oklahoma Medical Research Foundation and Department of Medicine, Oklahoma University Health Sciences Center Oklahoma City, OK 73104, USA

Received August 11, 1982. Revised December 20, 1982. Accepted January 6, 1983.

The mammalian cell antigen reactive with the autoantibody anti-jo-1 has been shown to contain tRNARis. The RNA sequence of this human and mouse cell tRNA was determined in a search for unusual features that might be realted to antigenicity. The 5' terminal nuleotide is unique among other sequenced tRNAs in that it is a methylated guanine. The presence of the hypermodified base quenine, which occurs in the wobble postition of the anticodon of tRNAHis from several species, was not detected in the tRNAHis immunoprecipitated by anti-jo-1 from either human HeLa or mouse Friend erytholeukeia cell extracts. The binding of protien(s) appears to confer antigenicity on tRNAHis since either protienase K treatment or phenol extraction resulted in the loss of immunoprecipatability. However, we have not suceeded in identifying an antigenic protien, and we find that the antigenic complex is not resolved from purified tRNAHis by Sepharcryl S-200 column chromatography. Immunofluorescence studies indicate that the antigenic from of tRNAHis is located preferentially in the mammalian cell cytoplasm. The results presented here are discussed in light of an earlier report (1) on the nature of the jo-1 antigen.

*Present address;Biogen Inc., 241 Binney St.,Cambridge, MA 02152, USA

**Department of MCD Biology, University of Colordo, Boulder, Co 80309, USA

+Department of Anatomy and Neurbiology, Washington University School of Medicine, ST. Louis Mo 63310, USA


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.