Ha. Thieringer et al., IDENTIFICATION AND DEVELOPMENTAL CHARACTERIZATION OF A NOVEL Y-BOX PROTEIN FROM DROSOPHILA-MELANOGASTER, Nucleic acids research, 25(23), 1997, pp. 4764-4770
The Y-box proteins are a family of highly conserved nucleic acid bindi
ng proteins which are conserved from bacteria to human. In this report
we have identified a new member of this family from Drosophila melano
gaster. Degenerate-PCR was used to identify a conserved region within
the highly conserved cold-shock domain (CSD) of Y-box proteins. Subseq
uently, the cDNA for this gene was sequenced, and the identified open
reading frame was named ypsilon schachtel (yps). The expression patter
n of yps indicates that this gene is expressed throughout development
with the highest level of expression found in adult flies, In situ hyb
ridization shows that the yps mRNA is maternally loaded into the egg c
ytoplasm. In addition, there appears to be expression of yps mRNA in m
esodermal tissue during embryogenesis. YPS, while containing a conserv
ed CSD, is novel in that it completely lacks the alternating acidic an
d basic regions found in the C-terminus of the other vertebrate eukary
otic Y-box proteins. The CSD of yps was purified and gel-shift analysi
s showed that this domain can interact with RNA, We predict that YPS w
ould be an RNA-binding protein due to these results and the motifs whi
ch have been identified within the amino acid sequence.