Cell-free translation of the mRNAs for the heavy and light chains of HLA-A and HLA-B antigens.
- 1 May 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (5), 2273-2277
- https://doi.org/10.1073/pnas.76.5.2273
Abstract
Cell-free translation of poly(A)-containing RNA from the JY lymphoblastoid cell line followed by immunoprecipitation has indicated the presence of mRNAs for both the heavy and light chains of HLA-A and HLA-B antigens in these preparations. Both chains are synthesized with an NH2-terminal extension, approximately 20 residues in length for the light chain, and 20 or 24 residues for the heavy chains. The precursors can be processed by dog pancreatic microsomes to products similar to those obtained in vivo. Immunoprecipitation of the cell-free products has been employed as an assay for partial purification of the mRNAs. Investigation of the Daudi cell line, which cannot synthesize the small subunit, beta 2-microglobin, has indicated that the heavy chains of HLA-A and HLA-B antigens are synthesized intracellularly in vivo and can also be translated from their cognate RNAs in vitro. The implications of these findings for biosynthesis of membrane proteins in general and multimeric membrane proteins in particular, as well as the role of beta 2-microglobulin in expression of HLA-A and HLA-B antigens, are discussed.This publication has 24 references indexed in Scilit:
- A signal sequence for the insertion of a transmembrane glycoprotein. Similarities to the signals of secretory proteins in primary structure and function.Journal of Biological Chemistry, 1978
- Glycosylation of a membrane protein is restricted to the growing polypeptide chain but is not necessary for insertion as a transmembrane proteinCell, 1978
- Isolation of separate mRNAs for α- and β-Tubulin and characterization of the corresponding in vitro translation productsCell, 1978
- Primary structures of N-terminal extra peptide segments linked to the variable and constant regions of immunoglobulin light chain precursors: implications on the organization and controlled expression of immunoglobulin genesBiochemistry, 1978
- Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysisCell, 1978
- The Genetic Control of HLA‐A and B Antigens in Somatic Cell Hybrids: Requirement for β2 MicroglobulinTissue Antigens, 1978
- Carbohydrate moiety of HLA antigens. Antigenic properties and amino acid sequences around the site of glycosylation.Journal of Biological Chemistry, 1977
- Structure of HL-A A and B Antigens Isolated from Cultured Human LymphocytesPublished by Cold Spring Harbor Laboratory ,1977
- Cell Membrane Antigen Isolation with the Staphylococcal Protein A-Antibody AdsorbentThe Journal of Immunology, 1976
- Independent expression of the two HL‐A antigen polypeptide chainsEuropean Journal of Immunology, 1975