Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble
Dribble (DBE) is an essential protein in Drosophila that belongs to the evolutionarily conserved Krr1p protein family. Proteins in this family are localised in the cell nucleolus and are important for the processing of ribosomal RNAs. However, little is known about their structural and biophysical p...
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| Published in: | Biochemical and biophysical research communications Vol. 343; no. 1; pp. 311 - 318 |
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| Abstract | Dribble (DBE) is an essential protein in
Drosophila that belongs to the evolutionarily conserved Krr1p protein family. Proteins in this family are localised in the cell nucleolus and are important for the processing of ribosomal RNAs. However, little is known about their structural and biophysical properties. We have expressed and purified full-length DBE protein from
Escherichia coli. Consistent with the native role of DBE in RNA processing, recombinant DBE was shown to bind RNA homo-polymers in vitro. By bioinformatics, size-exclusion chromatography, equilibrium sedimentation analysis, controlled proteolysis, and a variety of spectroscopic techniques, we have found that DBE is a monomeric protein in solution containing both α- and β-structures. Moreover, the structure of DBE is expanded and significantly disordered (∼45% disordered). Natively disordered proteins are thought to provide a disproportionately large surface area and structural plasticity for nucleic acid binding. We therefore propose that the presence of structural disorder is an important feature of DBE that facilitates the protein to interact with RNAs in the nucleolus. |
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| AbstractList | Dribble (DBE) is an essential protein in Drosophila that belongs to the evolutionarily conserved Krr1p protein family. Proteins in this family are localised in the cell nucleolus and are important for the processing of ribosomal RNAs. However, little is known about their structural and biophysical properties. We have expressed and purified full-length DBE protein from Escherichia coli. Consistent with the native role of DBE in RNA processing, recombinant DBE was shown to bind RNA homo-polymers in vitro. By bioinformatics, size-exclusion chromatography, equilibrium sedimentation analysis, controlled proteolysis, and a variety of spectroscopic techniques, we have found that DBE is a monomeric protein in solution containing both alpha- and beta-structures. Moreover, the structure of DBE is expanded and significantly disordered (approximately 45% disordered). Natively disordered proteins are thought to provide a disproportionately large surface area and structural plasticity for nucleic acid binding. We therefore propose that the presence of structural disorder is an important feature of DBE that facilitates the protein to interact with RNAs in the nucleolus. Dribble (DBE) is an essential protein in Drosophila that belongs to the evolutionarily conserved Krr1p protein family. Proteins in this family are localised in the cell nucleolus and are important for the processing of ribosomal RNAs. However, little is known about their structural and biophysical properties. We have expressed and purified full-length DBE protein from Escherichia coli. Consistent with the native role of DBE in RNA processing, recombinant DBE was shown to bind RNA homo-polymers in vitro. By bioinformatics, size-exclusion chromatography, equilibrium sedimentation analysis, controlled proteolysis, and a variety of spectroscopic techniques, we have found that DBE is a monomeric protein in solution containing both α- and β-structures. Moreover, the structure of DBE is expanded and significantly disordered (∼45% disordered). Natively disordered proteins are thought to provide a disproportionately large surface area and structural plasticity for nucleic acid binding. We therefore propose that the presence of structural disorder is an important feature of DBE that facilitates the protein to interact with RNAs in the nucleolus. Dribble (DBE) is an essential protein in Drosophila that belongs to the evolutionarily conserved Krr1p protein family. Proteins in this family are localised in the cell nucleolus and are important for the processing of ribosomal RNAs. However, little is known about their structural and biophysical properties. We have expressed and purified full-length DBE protein from Escherichia coli. Consistent with the native role of DBE in RNA processing, recombinant DBE was shown to bind RNA homo-polymers in vitro. By bioinformatics, size-exclusion chromatography, equilibrium sedimentation analysis, controlled proteolysis, and a variety of spectroscopic techniques, we have found that DBE is a monomeric protein in solution containing both alpha - and beta -structures. Moreover, the structure of DBE is expanded and significantly disordered (~45% disordered). Natively disordered proteins are thought to provide a disproportionately large surface area and structural plasticity for nucleic acid binding. We therefore propose that the presence of structural disorder is an important feature of DBE that facilitates the protein to interact with RNAs in the nucleolus. |
| Author | Yiu, C.-P. Benny Chan, H.Y. Edwin Beavil, Rebecca L. |
| Author_xml | – sequence: 1 givenname: C.-P. Benny surname: Yiu fullname: Yiu, C.-P. Benny organization: Laboratory of Drosophila Research, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China – sequence: 2 givenname: Rebecca L. surname: Beavil fullname: Beavil, Rebecca L. organization: The Randall Division, King’s College London, Guy’s Campus, London Bridge, London SE1 1UL, UK – sequence: 3 givenname: H.Y. Edwin surname: Chan fullname: Chan, H.Y. Edwin email: hyechan@cuhk.edu.hk organization: Laboratory of Drosophila Research, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16542639$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1110/ps.4210102 10.1016/S0968-0004(03)00003-3 10.1128/MCB.17.10.5707 10.1002/prot.10437 10.1021/bi011994o 10.1021/bi012159+ 10.1046/j.1365-2443.2000.00344.x 10.1038/nature03207 10.1091/mbc.12.5.1409 10.1016/j.febslet.2004.08.086 10.1006/jmbi.1996.0399 10.1128/MCB.20.21.7971-7979.2000 10.1016/0092-8674(94)90232-1 10.1093/molbev/msi052 10.1016/S0968-0004(02)02169-2 10.1016/S0092-8674(00)80668-6 10.1016/j.str.2005.04.008 10.1021/bi00211a042 10.1016/S0969-2126(99)80025-2 10.1093/nar/29.3.638 10.1128/MCB.18.8.4863 10.1021/bi961231e 10.1016/S0092-8674(00)81100-9 10.1038/nsb899 10.1021/bi035118h 10.1016/j.sbi.2005.01.002 10.1093/bioinformatics/18.1.211 |
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| Keywords | Pfg27 Intrinsically unfolded proteins K-homology Intrinsically disordered protein HRB2 Krr1p RNA binding |
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| Snippet | Dribble (DBE) is an essential protein in
Drosophila that belongs to the evolutionarily conserved Krr1p protein family. Proteins in this family are localised in... Dribble (DBE) is an essential protein in Drosophila that belongs to the evolutionarily conserved Krr1p protein family. Proteins in this family are localised in... |
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| SubjectTerms | Amino Acid Sequence Animals Biophysical Phenomena Biophysics Drosophila Drosophila melanogaster - metabolism Drosophila Proteins - biosynthesis Drosophila Proteins - chemistry Drosophila Proteins - genetics Escherichia coli HRB2 Intrinsically disordered protein Intrinsically unfolded proteins K-homology Krr1p Molecular Sequence Data Nuclear Proteins - biosynthesis Nuclear Proteins - chemistry Nuclear Proteins - genetics Pfg27 Protein Conformation RNA - chemistry RNA binding RNA-Binding Proteins - biosynthesis RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics Solvents - chemistry |
| Title | Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble |
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