Nucleic Acids Research, Vol 25, Issue 23 4764-4770, Copyright © 1997 by Oxford University Press
HA Thieringer, K Singh, H Trivedi and M Inouye
The Y-box proteins are a family of highly conserved nucleic acid binding
proteins which are conserved from bacteria to human. In this report we have
identified a new member of this family from Drosophila melanogaster.
Degenerate-PCR was used to identify a conserved region within the highly
conserved cold-shock domain (CSD) of Y-box proteins. Subsequently, the cDNA
for this gene was sequenced, and the identified open reading frame was
named ypsilon schachtel (yps). The expression pattern of yps indicates that
this gene is expressed throughout development with the highest level of
expression found in adult flies. In situ hybridization shows that the yps
mRNA is maternally loaded into the egg cytoplasm. In addition, there
appears to be expression of yps mRNA in mesodermal tissue during
embryogenesis. YPS, while containing a conserved CSD, is novel in that it
completely lacks the alternating acidic and basic regions found in the
C-terminus of the other vertebrate eukaryotic Y-box proteins. The CSD of
yps was purified and gel-shift analysis showed that this domain can
interact with RNA. We predict that YPS would be an RNA-binding protein due
to these results and the motifs which have been identified within the amino
acid sequence.
ARTICLES
Identification and developmental characterization of a novel Y-box protein from Drosophila melanogaster
Department of Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA.
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