TY - JOUR
T1 - Identification and developmental characterization of a novel Y-box protein from Drosophila melanogaster
AU - Thieringer, Heather A.
AU - Singh, Komal
AU - Trivedi, Harsh
AU - Inouye, Masayori
N1 - Funding Information:
We would like to thank Dr Marilyn Sanders for providing us with the Kc cell line and for supplying the cDNA library. We are indebted to the many Drosophila researchers at the Waksman Institute. In particular we would like to thank the laboratory of Dr Richard Padgett and particularly, Dr Janet Mullen for helping us with the whole mount in situ hybridization. We would also like to thank Dr Ruth Steward and the members of her laboratory for their help with the polytene chromosome hybridization, and for use of their microscope. In addition we acknowledge Dr Marcelo Jacobs-Lorena (Case Western Reserve University) for providing us with the frozen embryos, larvae and adult flies. Finally, we would like to thank Dr Ujwal Shinde for his help with computer imaging and Dr Sue Harlocker for her help with computer analysis. This work was supported by a grant issued from the National Institute of Health, GM19043.
PY - 1997
Y1 - 1997
N2 - 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.
AB - 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.
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U2 - 10.1093/nar/25.23.4764
DO - 10.1093/nar/25.23.4764
M3 - Article
C2 - 9365254
AN - SCOPUS:0030716829
SN - 0305-1048
VL - 25
SP - 4764
EP - 4770
JO - Nucleic acids research
JF - Nucleic acids research
IS - 23
ER -