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Bautz, Ekkehard K. F. [Editor]; Heidelberger Akademie der Wissenschaften / Mathematisch-Naturwissenschaftliche Klasse [VerfasserIn] [Editor]
Sitzungsberichte der Heidelberger Akademie der Wissenschaften, Mathematisch-Naturwissenschaftliche Klasse (1989, 4. Abhandlung): Molecular and cell biology of autoantibodies and autoimmunity: abstracts, 1. international workshop, July 27 - 29, 1989, Heidelberg — Berlin, Heidelberg [u.a.]: Springer, 1989

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https://doi.org/10.11588/diglit.48120#0131
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Abstracts

113

tigenic proteins do not contain an RRM, this possibility appears remote. One
epitope identified by Van Venrooij and coworkers resides within the RRM of
the A protein and also reacts with the B" protein. However, these antibodies do
not seem to recognize other members of the RRM family. It cannot be ruled out
at this time whether antibodies that cross-react within RRM are present at early
stages in the development of autoimmune disease and then disappear at later
times.
The autoantigenic members of the RRM family of proteins appear to be com-
mon to most tissues and conserved among metazoans. They probably constitute
important housekeeping functions that are required for constitutive RNA
metabolic processes. Recently, other members of the family have become evident
that may interact with or modify the normal functioning of the constitutive RNA
processing functions. For example, the Drosophila proteins involved in sex deter-
mination, and perhaps, some viral proteins may influence the pattern of splice site
selection through interactions with components of the small nuclear RNPs, in
particular, the 70 K protein of U 1 snRNPs. Some of these proteins include the
transformer, transformer-2, and sex-lethal proteins, as well as, gag gene products
of retroviruses. Transformer-2 and sex-lethal proteins contain RRM sequences
and presumably interact directly with RNA (see figure), while transformer and
gag contain arginine-rich (RD/RS/RE) sequences similar to those present in the
carboxyl region of 70 K, but lack an RRM. The sequence relationships and the
proposed trans-acting functions exhibited by these proteins in the determination
of splice site selection will be discussed. Below is a diagramatic representation of

RRM Family Proteins
 
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