Abstract
We have isolated a Drosophila melanogaster cDNA encoding a high-mobility-group (HMG) box-containing protein. This protein shares 50% amino acid identity with the human putative structure-specific recognition protein, hSSRP. The gene encoding the D. melanogaster homolog, DssRP, is developmentally regulated and is expressed most abundantly in ovaries (nurse cells in particular). The protein is localized in nuclei and is particularly abundant in the nucleolus. In vitro binding studies using DssRP produced in bacteria showed that, despite expectation, the protein does not bind to structured DNA. Instead, it binds to single-stranded DNA and RNA, with highest affinity to nucleotides G and U.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cell Compartmentation*
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Cell Nucleolus / chemistry*
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DNA, Single-Stranded / metabolism*
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DNA-Binding Proteins / genetics*
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DNA-Binding Proteins / metabolism
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Drosophila Proteins*
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Drosophila melanogaster / genetics*
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Female
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Gene Library
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High Mobility Group Proteins / genetics*
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High Mobility Group Proteins / metabolism
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Molecular Sequence Data
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RNA / metabolism
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RNA, Messenger / isolation & purification
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RNA-Binding Proteins / genetics*
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RNA-Binding Proteins / metabolism
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Recombinant Proteins / biosynthesis
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Sequence Homology, Amino Acid
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Transcriptional Elongation Factors*
Substances
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DNA, Single-Stranded
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DNA-Binding Proteins
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Drosophila Proteins
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High Mobility Group Proteins
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RNA, Messenger
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RNA-Binding Proteins
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Recombinant Proteins
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SSRP protein, Drosophila
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Transcriptional Elongation Factors
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RNA