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J. Biol. Chem., Vol. 275, Issue 37, 28583-28592, September 15, 2000
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From the Department of Biochemistry and Molecular Biology and
Feist-Weiller Cancer Center, Louisiana State University, Health
Sciences Center, Shreveport, Lousiana 71130
The post-transcriptional regulation of gene
expression by RNA-binding proteins is an important element in
controlling both normal cell functions and animal development. The
diverse roles are demonstrated by the Elav family of RNA-binding
proteins, where various members have been shown to regulate several
processes involving mRNA. We have identified another family of
RNA-binding proteins distantly related to the Elav family but closely
related to Bruno, a translational regulator in Drosophila
melanogaster. In humans, six Bruno-like genes have been
identified, whereas other species such as Drosophila,
Xenopus laevis, and Caenorhabditis elegans have
at least two members of this family, and related genes have also been
detected in plants and ascidians. The human BRUNOL2 and BRUNOL3 are
92% identical in the RNA-binding domains, although the
BRUNOL2 gene is expressed ubiquitously whereas
BRUNOL3 is expressed predominantly in the heart, muscle,
and nervous system. Both of these proteins bind the same target RNA,
the Bruno response element. The RNA-binding domain that recognizes the
Bruno response element is composed of two consecutive RNA recognition
motifs at the amino terminus of vertebrate Bruno protein. The possible involvement of the Bruno family of proteins in the CUG repeat expansion
disease myotonic dystrophy is discussed.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) C. elegans etr-1, U53931; Hu BRUNOL1, AF284423; Hu
BRUNOL2, AF248648, Hu BRUNOL3, U69546; Hu BRUNOL4, AF248649 and AF248650; and Hu BRUNOL5, AF248651.
A Family of Human RNA-binding Proteins Related to the
Drosophila Bruno Translational Regulator*
,
*
This work was supported by the American Heart Association,
Louisiana Affiliate, and the LSUHSC/Biomedical Research Foundation Stiles Trust Fund.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biochemistry
and Molecular Biology, Louisiana State University Health Sciences
Center, 1501 Kings Hwy., Shreveport, LA 71130. Tel.: 318-675-7829; Fax:
318-675-5180; E-mail: pgood@lsuhsc.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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