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Two cDNA clones, pDRH1 and pDRH2, containing sequences specific for human HLA-DR antigens were isolated from a bank of cDNA clones made from partially purified HLA-DR mRNA from the human lymphoblastoid cell line Maja. The clones were specific for the Mr 34,000 HLA-DR antigen glycoprotein chain. The identity of these clones was established by (i) their ability to hybridize specifically to HLA-DR mRNA in a positive selection assay; (ii) mRNA species hybridizing to the cDNA clones were expressed in B-cell but not in T-cell or fibroblast cell cultures; and (iii) a nucleotide sequence in the longer clone, pDRH2, could be translated into an amino acid sequence that is identical to the limited NH2-terminal amino acid sequence available for the purified HLA-DR antigen Mr 34,000 chain. Analysis of DNA from human, mouse, and human--mouse somatic cell hybrid lines by Southern transfer of restriction endonuclease digests indicated that the HLA-DR heavy chain is encoded in chromosome 6. This finding is compatible with the location of at least one of the HLA-D/DR heavy chain genes within the HLA region. In addition, the sequences coding for HLA-DR heavy chain appear to be present in only one or a few copies in the genome and to be relatively simple in structure.

Original publication

DOI

10.1073/pnas.79.2.545

Type

Journal article

Journal

Proc Natl Acad Sci U S A

Publication Date

01/1982

Volume

79

Pages

545 - 549

Keywords

Amino Acid Sequence, Base Sequence, Cell Line, Cell-Free System, Chromosomes, Human, 6-12 and X, Cloning, Molecular, DNA, HLA-DR Antigens, Histocompatibility Antigens Class II, Humans, Macromolecular Substances, Molecular Weight, Plasmids, Protein Biosynthesis