A Drosophila single-strand DNA/RNA-binding factor contains a high-mobility-group box and is enriched in the nucleolus

Tien Hsu; Dennis L. King; Carole Labonne; Fotis C. Kafatos

doi:10.1073/pnas.90.14.6488

A Drosophila single-strand DNA/RNA-binding factor contains a high-mobility-group box and is enriched in the nucleolus

Tien Hsu, Dennis L. King, Carole Labonne, Fotis C. Kafatos^*

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

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.

Original language	English (US)
Pages (from-to)	6488-6492
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	90
Issue number	14
DOIs	https://doi.org/10.1073/pnas.90.14.6488
State	Published - Jul 15 1993

Keywords

Drosophila nucleolar factor
Single-strand binding factor

ASJC Scopus subject areas

General

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title = "A Drosophila single-strand DNA/RNA-binding factor contains a high-mobility-group box and is enriched in the nucleolus",

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.",

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A Drosophila single-strand DNA/RNA-binding factor contains a high-mobility-group box and is enriched in the nucleolus. / Hsu, Tien; King, Dennis L.; Labonne, Carole; Kafatos, Fotis C.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 90, No. 14, 15.07.1993, p. 6488-6492.

Research output: Contribution to journal › Article › peer-review

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T1 - A Drosophila single-strand DNA/RNA-binding factor contains a high-mobility-group box and is enriched in the nucleolus

AU - Hsu, Tien

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AU - Kafatos, Fotis C.

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N2 - 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.

AB - 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.

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