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J. Biol. Chem., Vol. 263, Issue 34, 18043-18051, Dec, 1988
JC Chambers, D Kenan, BJ Martin and JD Keene
La is an autoimmune RNA-binding protein of 47 kDa that plays a role in the
transcription of RNA polymerase III. Both genomic and complementary DNAs
were isolated that encompass the coding sequence of the human La molecule.
The genomic clones encompass 11 exons and a putative G/C-rich promoter
upstream of the mRNA start site. The cDNA sequence encodes a protein of 408
amino acids and can be divided into two structural domains based upon amino
acid content and protease sensitivity. An unusually long stretch of 130
amino acids, much of which was predicted to form a stable alpha-helix, was
found near the middle of the protein between the two domains. A
ribonucleoprotein (RNP) consensus sequence was found just NH2-terminal to
the long alpha-helix. The RNP consensus sequence is split into two exons by
the fifth intron. Expression of three separate fragments of the La protein
in Escherichia coli showed that a strongly autoimmune-reactive portion
resides in the fragment containing the RNP consensus sequence and most of
the long alpha- helical core. Autoantibodies from La patients also reacted
with the terminal regions of the protein, but the extent of reactivity
varied among patients. Differences in reactivity of autoantibodies to each
portion of La protein may reflect an evolution of recognition of different
epitopes during the development of the autoimmune response. These findings
support an antigen-driven mechanism for autoimmune reactivity.
Genomic structure and amino acid sequence domains of the human La autoantigen
Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 27710.
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